ID CO4A3_HUMAN Reviewed; 1670 AA. AC Q01955; Q53QQ1; Q53R14; Q53RW8; Q9BQT2; Q9NYC4; Q9UDJ9; Q9UDK9; Q9UDL0; AC Q9UDL1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 3. DT 27-MAR-2024, entry version 240. DE RecName: Full=Collagen alpha-3(IV) chain; DE AltName: Full=Goodpasture antigen; DE Contains: DE RecName: Full=Tumstatin; DE Flags: Precursor; GN Name=COL4A3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS RP PRO-141; GLY-162 AND LEU-574. RC TISSUE=Kidney; RX PubMed=8083201; DOI=10.1016/s0021-9258(17)31612-5; RA Mariyama M., Leinonen A., Mochizuki T., Tryggvason K., Reeders S.T.; RT "Complete primary structure of the human alpha 3(IV) collagen chain. RT Coexpression of the alpha 3(IV) and alpha 4(IV) collagen chains in human RT tissues."; RL J. Biol. Chem. 269:23013-23017(1994). RN [2] RP SEQUENCE REVISION. RA Leinonen A.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ATS2 GLU-297; RP ARG-407; ARG-640; GLU-1207; GLN-1215; SER-1277; THR-1330; GLU-1334; RP GLU-1347 AND CYS-1661, VARIANT ATS3A ARG-1167, AND VARIANTS ARG-43; RP PRO-141; TYR-326; HIS-408; ARG-451; LEU-574; GLU-1269 AND PRO-1474. RX PubMed=11134255; DOI=10.1681/asn.v12197; RA Heidet L., Arrondel C., Forestier L., Cohen-Solal L., Mollet G., RA Gutierrez B., Stavrou C., Gubler M.-C., Antignac C.; RT "Structure of the human type IV collagen gene COL4A3 and mutations in RT autosomal Alport syndrome."; RL J. Am. Soc. Nephrol. 12:97-106(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. RX PubMed=9537506; DOI=10.1016/s0014-5793(98)00128-8; RA Momota R., Sugimoto M., Oohashi T., Kigasawa K., Yoshioka H., Ninomiya Y.; RT "Two genes, COL4A3 and COL4A4 coding for the human alpha3(IV) and RT alpha4(IV) collagen chains are arranged head-to-head on chromosome 2q36."; RL FEBS Lett. 424:11-16(1998). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1331-1670 (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=1737849; DOI=10.1172/jci115625; RA Turner N., Mason P.J., Brown R., Fox M., Povey S., Rees A., Pusey C.D.; RT "Molecular cloning of the human Goodpasture antigen demonstrates it to be RT the alpha 3 chain of type IV collagen."; RL J. Clin. Invest. 89:592-601(1992). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1386-1670 (ISOFORM 1), AND PARTIAL PROTEIN RP SEQUENCE. RX PubMed=1400291; DOI=10.1016/s0021-9258(19)88621-0; RA Quinones S., Bernal D., Garcia-Sogo M., Elena S.F., Saus J.; RT "Exon/intron structure of the human alpha 3(IV) gene encompassing the RT Goodpasture antigen (alpha 3(IV)NC1). Identification of a potentially RT antigenic region at the triple helix/NC1 domain junction."; RL J. Biol. Chem. 267:19780-19784(1992). RN [8] RP ERRATUM OF PUBMED:1400291. RX PubMed=8006044; DOI=10.1016/s0021-9258(17)32561-9; RA Quinones S., Bernal D., Garcia-Sogo M., Elena S.F., Saus J.; RL J. Biol. Chem. 269:17358-17358(1994). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1386-1670 (ISOFORMS 1; 2; 3; 4 AND 5), AND RP ALTERNATIVE SPLICING. RC TISSUE=Kidney; RX PubMed=7758473; DOI=10.1111/j.1432-1033.1995.tb20524.x; RA Penades J.R., Bernal D., Revert F., Johansson C., Fresquet V.J., RA Cervera J., Wieslander J., Quinones S., Saus J.; RT "Characterization and expression of multiple alternatively spliced RT transcripts of the Goodpasture antigen gene region. Goodpasture antibodies RT recognize recombinant proteins representing the autoantigen and one of its RT alternative forms."; RL Eur. J. Biochem. 229:754-760(1995). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1426-1670 (ISOFORM 1), AND FUNCTION. RX PubMed=10766752; DOI=10.1074/jbc.m001956200; RA Maeshima Y., Colorado P.C., Torre A., Holthaus K.A., Grunkemeyer J.A., RA Ericksen M.B., Hopfer H., Xiao Y., Stillman I.E., Kalluri R.; RT "Distinct antitumor properties of a type IV collagen domain derived from RT basement membrane."; RL J. Biol. Chem. 275:21340-21348(2000). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1439-1670 (ISOFORMS 2 AND 3), AND ALTERNATIVE RP SPLICING (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=8294492; DOI=10.1016/s0021-9258(17)42173-9; RA Feng L., Xia Y., Wilson C.B.; RT "Alternative splicing of the NC1 domain of the human alpha 3(IV) collagen RT gene. Differential expression of mRNA transcripts that predict three RT protein variants with distinct carboxyl regions."; RL J. Biol. Chem. 269:2342-2348(1994). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1453-1670 (ISOFORM 1). RX PubMed=1882840; RA Morrison K.E., Mariyama M., Yang-Feng T.L., Reeders S.T.; RT "Sequence and localization of a partial cDNA encoding the human alpha 3 RT chain of type IV collagen."; RL Am. J. Hum. Genet. 49:545-554(1991). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1644-1670 (ISOFORM 1). RC TISSUE=Kidney; RA Ding J.; RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases. RN [14] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE RP SPLICING, AND TISSUE SPECIFICITY. RC TISSUE=Kidney; RX PubMed=8505332; DOI=10.1016/s0021-9258(19)50312-x; RA Bernal D., Quinones S., Saus J.; RT "The human mRNA encoding the Goodpasture antigen is alternatively RT spliced."; RL J. Biol. Chem. 268:12090-12094(1993). RN [15] RP TISSUE SPECIFICITY. RX PubMed=7523402; DOI=10.1016/s0021-9258(18)47174-8; RA Leinonen A., Mariyama M., Mochizuki T., Tryggvason K., Reeders S.T.; RT "Complete primary structure of the human type IV collagen alpha 4(IV) RT chain. Comparison with structure and expression of the other alpha (IV) RT chains."; RL J. Biol. Chem. 269:26172-26177(1994). RN [16] RP PHOSPHORYLATION. RX PubMed=10212244; DOI=10.1074/jbc.274.18.12642; RA Raya A., Revert F., Navarro S., Saus J.; RT "Characterization of a novel type of serine/threonine kinase that RT specifically phosphorylates the human goodpasture antigen."; RL J. Biol. Chem. 274:12642-12649(1999). RN [17] RP FUNCTION. RX PubMed=10837460; DOI=10.1074/jbc.c000186200; RA Maeshima Y., Colorado P.C., Kalluri R.; RT "Two RGD-independent alpha vbeta 3 integrin binding sites on tumstatin RT regulate distinct anti-tumor properties."; RL J. Biol. Chem. 275:23745-23750(2000). RN [18] RP INVOLVEMENT IN ATS3A. RX PubMed=11044206; DOI=10.1111/j.1523-1755.2000.00358.x; RA van der Loop F.T.L., Heidet L., Timmer E.D.J., van den Bosch B.J.C., RA Leinonen A., Antignac C., Jefferson J.A., Maxwell A.P., Monnens L.A.H., RA Schroder C.H., Smeets H.J.M.; RT "Autosomal dominant Alport syndrome caused by a COL4A3 splice site RT mutation."; RL Kidney Int. 58:1870-1875(2000). RN [19] RP HEXAMERIZATION. RX PubMed=12193605; DOI=10.1074/jbc.m207769200; RA Borza D.B., Bondar O., Todd P., Sundaramoorthy M., Sado Y., Ninomiya Y., RA Hudson B.G.; RT "Quaternary organization of the goodpasture autoantigen, the alpha 3(IV) RT collagen chain. Sequestration of two cryptic autoepitopes by intrapromoter RT interactions with the alpha4 and alpha5 NC1 domains."; RL J. Biol. Chem. 277:40075-40083(2002). RN [20] RP FUNCTION, AND INTERACTION WITH ITGB3. RX PubMed=12682293; DOI=10.1073/pnas.0730882100; RA Sudhakar A., Sugimoto H., Yang C., Lively J., Zeisberg M., Kalluri R.; RT "Human tumstatin and human endostatin exhibit distinct antiangiogenic RT activities mediated by alpha v beta 3 and alpha 5 beta 1 integrins."; RL Proc. Natl. Acad. Sci. U.S.A. 100:4766-4771(2003). RN [21] RP FUNCTION. RX PubMed=15492988; DOI=10.1016/j.humpath.2004.06.008; RA Caudroy S., Cucherousset J., Lorenzato M., Zahm J.-M., RA Martinella-Catusse C., Polette M., Birembaut P.; RT "Implication of tumstatin in tumor progression of human bronchopulmonary RT carcinomas."; RL Hum. Pathol. 35:1218-1222(2004). RN [22] RP VARIANT PRO-1474. RX PubMed=7987301; DOI=10.1093/hmg/3.8.1269; RA Lemmink H.H., Mochizuki T., van den Heuvel L.P.W.J., Schroeder C.H., RA Barrientos A., Monnens L.A.H., van Oost B.A., Brunner H.G., Reeders S.T., RA Smeets H.J.M.; RT "Mutations in the type IV collagen alpha 3 (COL4A3) gene in autosomal RT recessive Alport syndrome."; RL Hum. Mol. Genet. 3:1269-1273(1994). RN [23] RP VARIANTS BFH2 VAL-985 AND GLU-1015. RX PubMed=11961012; DOI=10.1681/asn.v1351248; RA Badenas C., Praga M., Tazon B., Heidet L., Arrondel C., Armengol A., RA Andres A., Morales E., Camacho J.A., Lens X., Davila S., Mila M., RA Antignac C., Darnell A., Torra R.; RT "Mutations in the COL4A4 and COL4A3 genes cause familial benign RT hematuria."; RL J. Am. Soc. Nephrol. 13:1248-1254(2002). RN [24] RP VARIANTS ATS2 ASP-532; ARG-739; ARG-853 AND ARG-1216. RX PubMed=15954103; DOI=10.1002/humu.9349; RA Nagel M., Nagorka S., Gross O.; RT "Novel COL4A5, COL4A4, and COL4A3 mutations in Alport syndrome."; RL Hum. Mutat. 26:60-60(2005). RN [25] RP VARIANTS ATS2 VAL-631 AND CYS-1661. RX PubMed=29946535; DOI=10.3389/fped.2018.00171; RA Braunisch M.C., Buettner-Herold M., Guenthner R., Satanovskij R., RA Riedhammer K.M., Herr P.M., Klein H.G., Wahl D., Kuechle C., Renders L., RA Heemann U., Schmaderer C., Hoefele J.; RT "Heterozygous COL4A3 variants in histologically diagnosed focal segmental RT glomerulosclerosis."; RL Front. Pediatr. 6:171-171(2018). CC -!- FUNCTION: Type IV collagen is the major structural component of CC glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork CC together with laminins, proteoglycans and entactin/nidogen. CC -!- FUNCTION: Tumstatin, a cleavage fragment corresponding to the collagen CC alpha 3(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor CC cell activity; these two anti-tumor properties may be regulated via CC RGD-independent ITGB3-mediated mechanisms. CC -!- SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha CC 6(IV), each of which can form a triple helix structure with 2 other CC chains to generate type IV collagen network. The alpha 3(IV) chain CC forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this CC triple helical structure dimerizes through NC1-NC1 domain interactions CC such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one CC protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV) CC chains of the opposite promoter, respectively (PubMed:12193605). CC Interacts with ITGB3 (PubMed:12682293). Associates with LAMB2 at the CC neuromuscular junction and in GBM (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:12193605, ECO:0000269|PubMed:12682293}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. Note=Colocalizes with COL4A4 and COL4A5 in CC GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL). CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=The majority of isoforms differ in the C-terminal part of the CC NC1 domain.; CC Name=1; Synonyms=GP; CC IsoId=Q01955-1; Sequence=Displayed; CC Name=2; Synonyms=V, GP-V; CC IsoId=Q01955-2; Sequence=VSP_001170; CC Name=3; Synonyms=L5, GP-III, GP-III/V; CC IsoId=Q01955-3; Sequence=VSP_001171; CC Name=4; Synonyms=GP-III/IV/V; CC IsoId=Q01955-4; Sequence=VSP_023500; CC Name=5; Synonyms=GP-II/III/IV/V; CC IsoId=Q01955-5; Sequence=VSP_023498, VSP_023499; CC -!- TISSUE SPECIFICITY: Alpha 3 and alpha 4 type IV collagens are CC colocalized and present in kidney, eye, basement membranes of lens CC capsule, cochlea, lung, skeletal muscle, aorta, synaptic fibers, fetal CC kidney and fetal lung. PubMed:8083201 reports similar levels of CC expression of alpha 3 and alpha 4 type IV collagens in kidney, but CC PubMed:7523402 reports that in kidney levels of alpha 3 type IV CC collagen are significantly lower than those of alpha 4 type IV CC collagen. According to PubMed:8083201, alpha 3 type IV collagen is not CC detected in heart, brain, placenta, liver, pancreas, extrasynaptic CC muscle fibers, endoneurial and perineurial nerves, fetal brain, fetal CC heart and fetal liver. According to PubMed:7523402, alpha 3 type IV CC collagen is strongly expressed in pancreas, neuroretina and calvaria CC and not expressed in adrenal, ileum and skin. Isoform 1 and isoform 3 CC are strongly expressed in kidney, lung, suprarenal capsule, muscle and CC spleen, in each of these tissues isoform 1 is more abundant than CC isoform 3. Isoform 1 and isoform 3 are expressed at low levels in CC artery, fat, pericardium and peripherical nerve, but not in placenta, CC mesangium, skin, pleura and cultured umbilical endothelial cells. CC {ECO:0000269|PubMed:7523402, ECO:0000269|PubMed:8083201, CC ECO:0000269|PubMed:8505332}. CC -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain CC (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats CC in the long central triple-helical domain (which may cause flexibility CC in the triple helix), and a short N-terminal triple-helical 7S domain. CC -!- PTM: Prolines at the third position of the tripeptide repeating unit CC (G-X-Y) are hydroxylated in some or all of the chains. CC -!- PTM: Isoform 2 contains an additional N-linked glycosylation site. CC -!- PTM: Type IV collagens contain numerous cysteine residues which are CC involved in inter- and intramolecular disulfide bonding. 12 of these, CC located in the NC1 domain, are conserved in all known type IV CC collagens. CC -!- PTM: The trimeric structure of the NC1 domains is stabilized by CC covalent bonds between Lys and Met residues. {ECO:0000250}. CC -!- PTM: Phosphorylated. Thought to be phosphorylated by CERT, but CERT CC does not have kinase activity. {ECO:0000269|PubMed:10212244}. CC -!- DISEASE: Note=Autoantibodies against the NC1 domain of alpha 3(IV) are CC found in Goodpasture syndrome, an autoimmune disease of lung and CC kidney. CC -!- DISEASE: Alport syndrome 2, autosomal recessive (ATS2) [MIM:203780]: A CC syndrome characterized by progressive glomerulonephritis, glomerular CC basement membrane defects, renal failure, sensorineural deafness and CC specific eye abnormalities (lenticonous and macular flecks). The CC disorder shows considerable heterogeneity in that families differ in CC the age of end-stage renal disease and the occurrence of deafness. CC {ECO:0000269|PubMed:11134255, ECO:0000269|PubMed:15954103, CC ECO:0000269|PubMed:29946535}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Hematuria, benign familial, 2 (BFH2) [MIM:620320]: An CC autosomal dominant condition characterized by non-progressive isolated CC microscopic hematuria that does not result in renal failure. It is CC characterized pathologically by thinning of the glomerular basement CC membrane. {ECO:0000269|PubMed:11961012}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Alport syndrome 3A, autosomal dominant (ATS3A) [MIM:104200]: A CC form of Alport syndrome, a syndrome characterized by progressive CC glomerulonephritis, glomerular basement membrane defects, renal CC failure, sensorineural deafness and specific eye abnormalities CC (lenticonous and macular flecks). The disorder shows considerable CC heterogeneity in that families differ in the age of end-stage renal CC disease and the occurrence of deafness. {ECO:0000269|PubMed:11044206, CC ECO:0000269|PubMed:11134255}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: The epitopes recognized by the Goodpasture CC autoantibodies are sequestered within the NC1 hexamer of the type IV CC collagen network. CC -!- SIMILARITY: Belongs to the type IV collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00736}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X80031; CAA56335.1; -; mRNA. DR EMBL; AJ288487; CAC36101.1; -; Genomic_DNA. DR EMBL; AJ288488; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288489; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288490; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288491; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288492; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288493; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288494; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288495; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288496; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288497; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288498; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288499; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288500; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288501; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288502; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288503; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288504; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288505; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288506; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288507; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288508; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288509; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288510; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288511; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288512; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288513; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288514; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288515; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288516; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288517; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288518; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288519; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288520; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288521; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288522; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288523; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288524; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288525; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288526; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288527; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288528; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288529; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288530; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288531; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288532; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288533; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288534; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288535; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288536; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288537; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AJ288538; CAC36101.1; JOINED; Genomic_DNA. DR EMBL; AC079235; AAY14671.1; -; Genomic_DNA. DR EMBL; AC097662; AAY24251.1; -; Genomic_DNA. DR EMBL; AC107069; AAX93111.1; -; Genomic_DNA. DR EMBL; AB008496; BAA25064.1; -; Genomic_DNA. DR EMBL; M81379; AAA51556.1; -; mRNA. DR EMBL; M92993; AAA21610.1; -; mRNA. DR EMBL; AF258351; AAF72632.1; -; mRNA. DR EMBL; U02519; AAA18942.1; -; mRNA. DR EMBL; U02520; AAA18943.1; -; mRNA. DR EMBL; S55790; AAB19637.1; -; mRNA. DR EMBL; L08650; AAA52044.1; -; Genomic_DNA. DR CCDS; CCDS42829.1; -. [Q01955-1] DR PIR; A49736; A49736. DR PIR; A54763; CGHU3B. DR PIR; B49736; B49736. DR PIR; S69113; S69113. DR RefSeq; NP_000082.2; NM_000091.4. [Q01955-1] DR PDB; 5NB0; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1441-1670. DR PDB; 6WKU; X-ray; 1.76 A; A=1439-1666. DR PDBsum; 5NB0; -. DR PDBsum; 6WKU; -. DR AlphaFoldDB; Q01955; -. DR SMR; Q01955; -. DR BioGRID; 107682; 8. DR ComplexPortal; CPX-1725; Collagen type IV trimer variant 3. DR CORUM; Q01955; -. DR IntAct; Q01955; 2. DR STRING; 9606.ENSP00000379823; -. DR ChEMBL; CHEMBL2364188; -. DR GlyCosmos; Q01955; 1 site, No reported glycans. DR GlyGen; Q01955; 1 site. DR iPTMnet; Q01955; -. DR PhosphoSitePlus; Q01955; -. DR BioMuta; COL4A3; -. DR DMDM; 134035067; -. DR EPD; Q01955; -. DR jPOST; Q01955; -. DR MassIVE; Q01955; -. DR MaxQB; Q01955; -. DR PaxDb; 9606-ENSP00000379823; -. DR PeptideAtlas; Q01955; -. DR ProteomicsDB; 58016; -. [Q01955-1] DR ProteomicsDB; 58017; -. [Q01955-2] DR ProteomicsDB; 58018; -. [Q01955-3] DR ProteomicsDB; 58019; -. [Q01955-4] DR ProteomicsDB; 58020; -. [Q01955-5] DR ABCD; Q01955; 1 sequenced antibody. DR Antibodypedia; 34379; 346 antibodies from 32 providers. DR DNASU; 1285; -. DR Ensembl; ENST00000396578.8; ENSP00000379823.3; ENSG00000169031.21. [Q01955-1] DR GeneID; 1285; -. DR KEGG; hsa:1285; -. DR MANE-Select; ENST00000396578.8; ENSP00000379823.3; NM_000091.5; NP_000082.2. DR UCSC; uc002vom.2; human. [Q01955-1] DR AGR; HGNC:2204; -. DR CTD; 1285; -. DR DisGeNET; 1285; -. DR GeneCards; COL4A3; -. DR GeneReviews; COL4A3; -. DR HGNC; HGNC:2204; COL4A3. DR HPA; ENSG00000169031; Tissue enhanced (kidney, retina). DR MalaCards; COL4A3; -. DR MIM; 104200; phenotype. DR MIM; 120070; gene. DR MIM; 203780; phenotype. DR MIM; 620320; phenotype. DR neXtProt; NX_Q01955; -. DR OpenTargets; ENSG00000169031; -. DR Orphanet; 88918; Autosomal dominant Alport syndrome. DR Orphanet; 88919; Autosomal recessive Alport syndrome. DR Orphanet; 653722; Digenic Alport syndrome. DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome. DR Orphanet; 97562; NON RARE IN EUROPE: Benign familial hematuria. DR PharmGKB; PA26719; -. DR VEuPathDB; HostDB:ENSG00000169031; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000161675; -. DR HOGENOM; CLU_002023_0_0_1; -. DR InParanoid; Q01955; -. DR OMA; KGPPGRC; -. DR OrthoDB; 2882192at2759; -. DR PhylomeDB; Q01955; -. DR TreeFam; TF344135; -. DR PathwayCommons; Q01955; -. DR Reactome; R-HSA-1442490; Collagen degradation. DR Reactome; R-HSA-1474244; Extracellular matrix organization. DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes. DR Reactome; R-HSA-186797; Signaling by PDGF. DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-2214320; Anchoring fibril formation. DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils. DR Reactome; R-HSA-3000157; Laminin interactions. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-419037; NCAM1 interactions. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR SignaLink; Q01955; -. DR SIGNOR; Q01955; -. DR BioGRID-ORCS; 1285; 10 hits in 1145 CRISPR screens. DR ChiTaRS; COL4A3; human. DR GeneWiki; Collagen_alpha-3(IV)_chain; -. DR GenomeRNAi; 1285; -. DR Pharos; Q01955; Tbio. DR PRO; PR:Q01955; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q01955; Protein. DR Bgee; ENSG00000169031; Expressed in skeletal muscle tissue of biceps brachii and 151 other cell types or tissues. DR ExpressionAtlas; Q01955; baseline and differential. DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB. DR GO; GO:0005587; C:collagen type IV trimer; IDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL. DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB. DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; NAS:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc. DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB. DR GO; GO:0008015; P:blood circulation; TAS:ProtInc. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB. DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl. DR GO; GO:0072577; P:endothelial cell apoptotic process; IDA:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR GO; GO:0032836; P:glomerular basement membrane development; ISS:UniProtKB. DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IDA:UniProtKB. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc. DR Gene3D; 2.170.240.10; Collagen IV, non-collagenous; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR001442; Collagen_IV_NC. DR InterPro; IPR036954; Collagen_IV_NC_sf. DR InterPro; IPR016187; CTDL_fold. DR PANTHER; PTHR24023:SF1019; COLLAGEN; 1. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR Pfam; PF01413; C4; 2. DR Pfam; PF01391; Collagen; 23. DR SMART; SM00111; C4; 2. DR SUPFAM; SSF56436; C-type lectin-like; 2. DR PROSITE; PS51403; NC1_IV; 1. DR Genevisible; Q01955; HS. PE 1: Evidence at protein level; KW 3D-structure; Alport syndrome; Alternative splicing; Basement membrane; KW Cell adhesion; Collagen; Deafness; Direct protein sequencing; KW Disease variant; Disulfide bond; Extracellular matrix; Glycoprotein; KW Hydroxylation; Phosphoprotein; Reference proteome; Repeat; Secreted; KW Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT CHAIN 29..1670 FT /note="Collagen alpha-3(IV) chain" FT /id="PRO_0000005844" FT CHAIN 1426..1670 FT /note="Tumstatin" FT /id="PRO_0000279684" FT DOMAIN 1445..1669 FT /note="Collagen IV NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT REGION 29..42 FT /note="7S domain" FT REGION 43..1438 FT /note="Triple-helical region" FT REGION 49..78 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 167..469 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 502..1442 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1427..1444 FT /note="Epitope recognized by Goodpasture antibodies" FT REGION 1479..1557 FT /note="Required for the anti-angiogenic activity of FT tumstatin" FT REGION 1610..1628 FT /note="Required for the anti-tumor cell activity of FT tumstatin" FT MOTIF 791..793 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 996..998 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1154..1156 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1306..1308 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1345..1347 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 1432..1434 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 178..204 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 363..383 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 427..442 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 600..619 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 651..674 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 690..709 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1092..1113 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1359..1387 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 1426..1427 FT /note="Cleavage; by collagenase" FT /evidence="ECO:0000250" FT CARBOHYD 253 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 1460..1551 FT /note="Or C-1460 with C-1548" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1493..1548 FT /note="Or C-1493 with C-1551" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1505..1511 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1570..1665 FT /note="Or C-1570 with C-1662" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1604..1662 FT /note="Or C-1604 with C-1665" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1616..1622 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT CROSSLNK 1533 FT /note="S-Lysyl-methionine sulfilimine (Met-Lys) (interchain FT with K-1651)" FT /evidence="ECO:0000250" FT CROSSLNK 1651 FT /note="S-Lysyl-methionine sulfilimine (Lys-Met) (interchain FT with M-1533)" FT /evidence="ECO:0000250" FT VAR_SEQ 1418..1424 FT /note="GPAGSDG -> ESLFHQL (in isoform 5)" FT /evidence="ECO:0000303|PubMed:7758473" FT /id="VSP_023498" FT VAR_SEQ 1425..1670 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:7758473" FT /id="VSP_023499" FT VAR_SEQ 1488..1670 FT /note="GTLGSCLQRFTTMPFLFCNVNDVCNFASRNDYSYWLSTPALMPMNMAPITGR FT ALEPYISRCTVCEGPAIAIAVHSQTTDIPPCPHGWISLWKGFSFIMFTSAGSEGTGQAL FT ASPGSCLEEFRASPFLECHGRGTCNYYSNSYSFWLASLNPERMFRKPIPSTVKAGELEK FT IISRCQVCMKKRH -> DALFVKVLRSP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:7758473, FT ECO:0000303|PubMed:8294492" FT /id="VSP_001171" FT VAR_SEQ 1488..1670 FT /note="GTLGSCLQRFTTMPFLFCNVNDVCNFASRNDYSYWLSTPALMPMNMAPITGR FT ALEPYISRCTVCEGPAIAIAVHSQTTDIPPCPHGWISLWKGFSFIMFTSAGSEGTGQAL FT ASPGSCLEEFRASPFLECHGRGTCNYYSNSYSFWLASLNPERMFRKPIPSTVKAGELEK FT IISRCQVCMKKRH -> ESLFHQL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:7758473" FT /id="VSP_023500" FT VAR_SEQ 1586..1670 FT /note="FTSAGSEGTGQALASPGSCLEEFRASPFLECHGRGTCNYYSNSYSFWLASLN FT PERMFRKPIPSTVKAGELEKIISRCQVCMKKRH -> KAYSINCESWGIRKNNKSLSGV FT HEEKTLKLKKTAELVFFILKNKVMTEHAVI (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7758473, FT ECO:0000303|PubMed:8294492" FT /id="VSP_001170" FT VARIANT 43 FT /note="G -> R (in dbSNP:rs13424243)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011202" FT VARIANT 141 FT /note="L -> P (in dbSNP:rs10178458)" FT /evidence="ECO:0000269|PubMed:11134255, FT ECO:0000269|PubMed:8083201" FT /id="VAR_030944" FT VARIANT 162 FT /note="E -> G (in dbSNP:rs6436669)" FT /evidence="ECO:0000269|PubMed:8083201" FT /id="VAR_011203" FT VARIANT 297 FT /note="G -> E (in ATS2; dbSNP:rs1422638161)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011204" FT VARIANT 326 FT /note="D -> Y (in dbSNP:rs55703767)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011205" FT VARIANT 407 FT /note="G -> R (in ATS2; dbSNP:rs1559878862)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011206" FT VARIANT 408 FT /note="R -> H (in dbSNP:rs34505188)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011207" FT VARIANT 451 FT /note="H -> R (in dbSNP:rs11677877)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011208" FT VARIANT 532 FT /note="G -> D (in ATS2; dbSNP:rs371405814)" FT /evidence="ECO:0000269|PubMed:15954103" FT /id="VAR_030945" FT VARIANT 574 FT /note="P -> L (in dbSNP:rs28381984)" FT /evidence="ECO:0000269|PubMed:11134255, FT ECO:0000269|PubMed:8083201" FT /id="VAR_011209" FT VARIANT 631 FT /note="G -> V (in ATS2; uncertain significance; FT dbSNP:rs1315862965)" FT /evidence="ECO:0000269|PubMed:29946535" FT /id="VAR_080826" FT VARIANT 640 FT /note="G -> R (in ATS2; dbSNP:rs200672668)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011210" FT VARIANT 739 FT /note="G -> R (in ATS2; dbSNP:rs375040636)" FT /evidence="ECO:0000269|PubMed:15954103" FT /id="VAR_030946" FT VARIANT 834 FT /note="K -> R (in dbSNP:rs56226424)" FT /id="VAR_061118" FT VARIANT 853 FT /note="G -> R (in ATS2; dbSNP:rs763726708)" FT /evidence="ECO:0000269|PubMed:15954103" FT /id="VAR_030947" FT VARIANT 985 FT /note="G -> V (in BFH2; dbSNP:rs121912827)" FT /evidence="ECO:0000269|PubMed:11961012" FT /id="VAR_030948" FT VARIANT 1015 FT /note="G -> E (in BFH2; dbSNP:rs121912826)" FT /evidence="ECO:0000269|PubMed:11961012" FT /id="VAR_030949" FT VARIANT 1167 FT /note="G -> R (in ATS3A; dbSNP:rs267606745)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011211" FT VARIANT 1207 FT /note="G -> E (in ATS2; in isolated microhematuria at FT heterozygosity; dbSNP:rs1553764136)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011212" FT VARIANT 1215 FT /note="R -> Q (in ATS2; uncertain significance; FT dbSNP:rs200443942)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011213" FT VARIANT 1216 FT /note="G -> R (in ATS2)" FT /evidence="ECO:0000269|PubMed:15954103" FT /id="VAR_030950" FT VARIANT 1269 FT /note="D -> E (in dbSNP:rs57611801)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011214" FT VARIANT 1277 FT /note="G -> S (in ATS2; dbSNP:rs190598500)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011215" FT VARIANT 1330 FT /note="I -> T (in ATS2; uncertain significance; FT dbSNP:rs767033956)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011216" FT VARIANT 1334 FT /note="G -> E (in ATS2; dbSNP:rs375290088)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011217" FT VARIANT 1347 FT /note="D -> E (in ATS2; uncertain significance; FT dbSNP:rs73996414)" FT /evidence="ECO:0000269|PubMed:11134255" FT /id="VAR_011218" FT VARIANT 1474 FT /note="L -> P (in dbSNP:rs200302125)" FT /evidence="ECO:0000269|PubMed:11134255, FT ECO:0000269|PubMed:7987301" FT /id="VAR_001908" FT VARIANT 1495 FT /note="Q -> R (in dbSNP:rs77964815)" FT /id="VAR_001909" FT VARIANT 1661 FT /note="R -> C (in ATS2; uncertain significance; FT dbSNP:rs201697532)" FT /evidence="ECO:0000269|PubMed:11134255, FT ECO:0000269|PubMed:29946535" FT /id="VAR_011219" FT CONFLICT 911 FT /note="T -> R (in Ref. 3; CAC36101)" FT /evidence="ECO:0000305" FT CONFLICT 1539 FT /note="R -> I (in Ref. 11; AAA18942)" FT /evidence="ECO:0000305" FT CONFLICT 1594 FT /note="T -> A (in Ref. 12; AAB19637)" FT /evidence="ECO:0000305" FT CONFLICT 1663..1664 FT /note="QV -> HL (in Ref. 13; AAA52044)" FT /evidence="ECO:0000305" FT STRAND 1445..1451 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1453..1456 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1465..1478 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1481..1484 FT /evidence="ECO:0007829|PDB:6WKU" FT HELIX 1490..1492 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1493..1496 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1502..1505 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1511..1514 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1519..1524 FT /evidence="ECO:0007829|PDB:6WKU" FT HELIX 1538..1544 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1547..1555 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1557..1561 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1563..1566 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1575..1587 FT /evidence="ECO:0007829|PDB:6WKU" FT HELIX 1589..1591 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1593..1595 FT /evidence="ECO:0007829|PDB:6WKU" FT HELIX 1601..1603 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1604..1607 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1613..1617 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1629..1634 FT /evidence="ECO:0007829|PDB:6WKU" FT HELIX 1638..1640 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1641..1643 FT /evidence="ECO:0007829|PDB:5NB0" FT STRAND 1648..1651 FT /evidence="ECO:0007829|PDB:6WKU" FT HELIX 1655..1658 FT /evidence="ECO:0007829|PDB:6WKU" FT STRAND 1661..1666 FT /evidence="ECO:0007829|PDB:6WKU" FT CONFLICT Q01955-2:1539 FT /note="R -> I (in Ref. 11; AAA18942)" FT /evidence="ECO:0000305" SQ SEQUENCE 1670 AA; 161813 MW; AA65D50903D82B99 CRC64; MSARTAPRPQ VLLLPLLLVL LAAAPAASKG CVCKDKGQCF CDGAKGEKGE KGFPGPPGSP GQKGFTGPEG LPGPQGPKGF PGLPGLTGSK GVRGISGLPG FSGSPGLPGT PGNTGPYGLV GVPGCSGSKG EQGFPGLPGT LGYPGIPGAA GLKGQKGAPA KEEDIELDAK GDPGLPGAPG PQGLPGPPGF PGPVGPPGPP GFFGFPGAMG PRGPKGHMGE RVIGHKGERG VKGLTGPPGP PGTVIVTLTG PDNRTDLKGE KGDKGAMGEP GPPGPSGLPG ESYGSEKGAP GDPGLQGKPG KDGVPGFPGS EGVKGNRGFP GLMGEDGIKG QKGDIGPPGF RGPTEYYDTY QEKGDEGTPG PPGPRGARGP QGPSGPPGVP GSPGSSRPGL RGAPGWPGLK GSKGERGRPG KDAMGTPGSP GCAGSPGLPG SPGPPGPPGD IVFRKGPPGD HGLPGYLGSP GIPGVDGPKG EPGLLCTQCP YIPGPPGLPG LPGLHGVKGI PGRQGAAGLK GSPGSPGNTG LPGFPGFPGA QGDPGLKGEK GETLQPEGQV GVPGDPGLRG QPGRKGLDGI PGTPGVKGLP GPKGELALSG EKGDQGPPGD PGSPGSPGPA GPAGPPGYGP QGEPGLQGTQ GVPGAPGPPG EAGPRGELSV STPVPGPPGP PGPPGHPGPQ GPPGIPGSLG KCGDPGLPGP DGEPGIPGIG FPGPPGPKGD QGFPGTKGSL GCPGKMGEPG LPGKPGLPGA KGEPAVAMPG GPGTPGFPGE RGNSGEHGEI GLPGLPGLPG TPGNEGLDGP RGDPGQPGPP GEQGPPGRCI EGPRGAQGLP GLNGLKGQQG RRGKTGPKGD PGIPGLDRSG FPGETGSPGI PGHQGEMGPL GQRGYPGNPG ILGPPGEDGV IGMMGFPGAI GPPGPPGNPG TPGQRGSPGI PGVKGQRGTP GAKGEQGDKG NPGPSEISHV IGDKGEPGLK GFAGNPGEKG NRGVPGMPGL KGLKGLPGPA GPPGPRGDLG STGNPGEPGL RGIPGSMGNM GMPGSKGKRG TLGFPGRAGR PGLPGIHGLQ GDKGEPGYSE GTRPGPPGPT GDPGLPGDMG KKGEMGQPGP PGHLGPAGPE GAPGSPGSPG LPGKPGPHGD LGFKGIKGLL GPPGIRGPPG LPGFPGSPGP MGIRGDQGRD GIPGPAGEKG ETGLLRAPPG PRGNPGAQGA KGDRGAPGFP GLPGRKGAMG DAGPRGPTGI EGFPGPPGLP GAIIPGQTGN RGPPGSRGSP GAPGPPGPPG SHVIGIKGDK GSMGHPGPKG PPGTAGDMGP PGRLGAPGTP GLPGPRGDPG FQGFPGVKGE KGNPGFLGSI GPPGPIGPKG PPGVRGDPGT LKIISLPGSP GPPGTPGEPG MQGEPGPPGP PGNLGPCGPR GKPGKDGKPG TPGPAGEKGN KGSKGEPGPA GSDGLPGLKG KRGDSGSPAT WTTRGFVFTR HSQTTAIPSC PEGTVPLYSG FSFLFVQGNQ RAHGQDLGTL GSCLQRFTTM PFLFCNVNDV CNFASRNDYS YWLSTPALMP MNMAPITGRA LEPYISRCTV CEGPAIAIAV HSQTTDIPPC PHGWISLWKG FSFIMFTSAG SEGTGQALAS PGSCLEEFRA SPFLECHGRG TCNYYSNSYS FWLASLNPER MFRKPIPSTV KAGELEKIIS RCQVCMKKRH //