ID   CO8A1_HUMAN             Reviewed;         744 AA.
AC   P27658; D3DN42; Q53XI6; Q96D07;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   27-MAR-2024, entry version 208.
DE   RecName: Full=Collagen alpha-1(VIII) chain;
DE   AltName: Full=Endothelial collagen;
DE   Contains:
DE     RecName: Full=Vastatin;
DE   Flags: Precursor;
GN   Name=COL8A1; Synonyms=C3orf7;
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].
RX   PubMed=2029894; DOI=10.1111/j.1432-1033.1991.tb15951.x;
RA   Muragaki Y., Mattei M.-G., Yamaguchi N., Olsen B.R., Ninomiya Y.;
RT   "The complete primary structure of the human alpha 1 (VIII) chain and
RT   assignment of its gene (COL8A1) to chromosome 3.";
RL   Eur. J. Biochem. 197:615-622(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=2376131; DOI=10.3109/03008209009152157;
RA   Kittelberger R., Davis P.F., Flynn D.W., Greenhill N.S.;
RT   "Distribution of type VIII collagen in tissues: an immunohistochemical
RT   study.";
RL   Connect. Tissue Res. 24:303-318(1990).
RN   [6]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=1515454; DOI=10.1016/0925-4439(92)90103-t;
RA   Kittelberger R., Neale T.J., Francky K.T., Greenhill N.S., Gibson G.J.;
RT   "Cleavage of type VIII collagen by human neutrophil elastase.";
RL   Biochim. Biophys. Acta 1139:295-299(1992).
RN   [7]
RP   TISSUE SPECIFICITY, AND POSSIBLE FUNCTION.
RX   PubMed=7734329;
RA   Ruger B., Dunbar P.R., Hasan Q., Sawada H., Kittelberger R., Greenhill N.,
RA   Neale T.J.;
RT   "Human mast cells produce type VIII collagen in vivo.";
RL   Int. J. Exp. Pathol. 75:397-404(1994).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=10686422; DOI=10.1016/s0945-053x(99)00053-0;
RA   Greenhill N.S., Ruger B.M., Hasan Q., Davis P.F.;
RT   "The alpha1(VIII) and alpha2(VIII) collagen chains form two distinct
RT   homotrimeric proteins in vivo.";
RL   Matrix Biol. 19:19-28(2000).
RN   [9]
RP   FUNCTION OF VASTATIN.
RX   PubMed=11708810; DOI=10.1006/bbrc.2001.5970;
RA   Xu R., Yao Z.-Y., Xin L., Zhang Q., Li T.-P., Gan R.-B.;
RT   "NC1 domain of human type VIII collagen (alpha 1) inhibits bovine aortic
RT   endothelial cell proliferation and causes cell apoptosis.";
RL   Biochem. Biophys. Res. Commun. 289:264-268(2001).
RN   [10]
RP   SUBUNIT.
RX   PubMed=14990571; DOI=10.1074/jbc.m305805200;
RA   Stephan S., Sherratt M.J., Hodson N., Shuttleworth C.A., Kielty C.M.;
RT   "Expression and supramolecular assembly of recombinant alpha1(viii) and
RT   alpha2(viii) collagen homotrimers.";
RL   J. Biol. Chem. 279:21469-21477(2004).
RN   [11]
RP   INDUCTION.
RX   PubMed=17888087; DOI=10.1111/j.1365-2362.2007.01864.x;
RA   Gerth J., Cohen C.D., Hopfer U., Lindenmeyer M.T., Sommer M., Grone H.J.,
RA   Wolf G.;
RT   "Collagen type VIII expression in human diabetic nephropathy.";
RL   Eur. J. Clin. Invest. 37:767-773(2007).
CC   -!- FUNCTION: Macromolecular component of the subendothelium. Major
CC       component of the Descemet's membrane (basement membrane) of corneal
CC       endothelial cells. Also a component of the endothelia of blood vessels.
CC       Necessary for migration and proliferation of vascular smooth muscle
CC       cells and thus, has a potential role in the maintenance of vessel wall
CC       integrity and structure, in particular in atherogenesis.
CC       {ECO:0000269|PubMed:11708810}.
CC   -!- FUNCTION: Vastatin, the C-terminal fragment comprising the NC1 domain,
CC       inhibits aortic endothelial cell proliferation and causes cell
CC       apoptosis. {ECO:0000269|PubMed:11708810}.
CC   -!- SUBUNIT: Homotrimers, or heterotrimers in association with alpha
CC       2(VIII) type collagens. Four homotrimers can form a tetrahedron
CC       stabilized by central interacting C-terminal NC1 trimers.
CC       {ECO:0000269|PubMed:14990571}.
CC   -!- INTERACTION:
CC       P27658; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-747133, EBI-11976299;
CC       P27658; Q96C12: ARMC5; NbExp=3; IntAct=EBI-747133, EBI-6425121;
CC       P27658; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-747133, EBI-953896;
CC       P27658; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-747133, EBI-7317823;
CC       P27658; P48745: CCN3; NbExp=3; IntAct=EBI-747133, EBI-3904822;
CC       P27658; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-747133, EBI-747776;
CC       P27658; Q9H5F2: CFAP68; NbExp=3; IntAct=EBI-747133, EBI-718615;
CC       P27658; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-747133, EBI-7062247;
CC       P27658; Q02930-3: CREB5; NbExp=6; IntAct=EBI-747133, EBI-10192698;
CC       P27658; A8MQ03: CYSRT1; NbExp=6; IntAct=EBI-747133, EBI-3867333;
CC       P27658; A0A0U1RQF7: DPEP2NB; NbExp=3; IntAct=EBI-747133, EBI-18398199;
CC       P27658; Q9NVL1-2: FAM86C1P; NbExp=5; IntAct=EBI-747133, EBI-12845222;
CC       P27658; P98095: FBLN2; NbExp=3; IntAct=EBI-747133, EBI-947973;
CC       P27658; Q9NWN3: FBXO34; NbExp=3; IntAct=EBI-747133, EBI-719816;
CC       P27658; O43559: FRS3; NbExp=3; IntAct=EBI-747133, EBI-725515;
CC       P27658; O76003: GLRX3; NbExp=3; IntAct=EBI-747133, EBI-374781;
CC       P27658; O15499: GSC2; NbExp=3; IntAct=EBI-747133, EBI-19954058;
CC       P27658; P49639: HOXA1; NbExp=6; IntAct=EBI-747133, EBI-740785;
CC       P27658; Q0VD86: INCA1; NbExp=9; IntAct=EBI-747133, EBI-6509505;
CC       P27658; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-747133, EBI-10693436;
CC       P27658; Q5T749: KPRP; NbExp=3; IntAct=EBI-747133, EBI-10981970;
CC       P27658; O76014: KRT37; NbExp=3; IntAct=EBI-747133, EBI-1045716;
CC       P27658; Q6A162: KRT40; NbExp=3; IntAct=EBI-747133, EBI-10171697;
CC       P27658; Q9NSB4: KRT82; NbExp=3; IntAct=EBI-747133, EBI-1045341;
CC       P27658; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-747133, EBI-11749135;
CC       P27658; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-747133, EBI-10172290;
CC       P27658; P60410: KRTAP10-8; NbExp=8; IntAct=EBI-747133, EBI-10171774;
CC       P27658; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-747133, EBI-11953334;
CC       P27658; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-747133, EBI-10241252;
CC       P27658; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-747133, EBI-12196745;
CC       P27658; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-747133, EBI-1048945;
CC       P27658; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-747133, EBI-10241353;
CC       P27658; Q6PEX3: KRTAP26-1; NbExp=4; IntAct=EBI-747133, EBI-3957672;
CC       P27658; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-747133, EBI-751260;
CC       P27658; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-747133, EBI-10250562;
CC       P27658; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-747133, EBI-11987425;
CC       P27658; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-747133, EBI-3958099;
CC       P27658; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-747133, EBI-11962084;
CC       P27658; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-747133, EBI-1044640;
CC       P27658; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-747133, EBI-1043191;
CC       P27658; P48059-3: LIMS1; NbExp=3; IntAct=EBI-747133, EBI-12864460;
CC       P27658; Q3KP22-3: MAJIN; NbExp=3; IntAct=EBI-747133, EBI-18015780;
CC       P27658; Q6IA69: NADSYN1; NbExp=3; IntAct=EBI-747133, EBI-748610;
CC       P27658; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-747133, EBI-945833;
CC       P27658; P0DPK4: NOTCH2NLC; NbExp=5; IntAct=EBI-747133, EBI-22310682;
CC       P27658; P32242: OTX1; NbExp=3; IntAct=EBI-747133, EBI-740446;
CC       P27658; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-747133, EBI-750734;
CC       P27658; Q8WVV4-1: POF1B; NbExp=3; IntAct=EBI-747133, EBI-11986735;
CC       P27658; Q12837: POU4F2; NbExp=5; IntAct=EBI-747133, EBI-17236143;
CC       P27658; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-747133, EBI-740343;
CC       P27658; Q04864: REL; NbExp=3; IntAct=EBI-747133, EBI-307352;
CC       P27658; O76081-6: RGS20; NbExp=3; IntAct=EBI-747133, EBI-10178530;
CC       P27658; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-747133, EBI-17589229;
CC       P27658; P78381-3: SLC35A2; NbExp=3; IntAct=EBI-747133, EBI-13307533;
CC       P27658; Q02446: SP4; NbExp=3; IntAct=EBI-747133, EBI-10198587;
CC       P27658; Q6RVD6: SPATA8; NbExp=3; IntAct=EBI-747133, EBI-8635958;
CC       P27658; Q8NCR6: SPMIP6; NbExp=3; IntAct=EBI-747133, EBI-10269322;
CC       P27658; Q9C004: SPRY4; NbExp=3; IntAct=EBI-747133, EBI-354861;
CC       P27658; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-747133, EBI-17716262;
CC       P27658; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-747133, EBI-947187;
CC       P27658; Q08AM6: VAC14; NbExp=7; IntAct=EBI-747133, EBI-2107455;
CC       P27658; Q8TCV5: WFDC5; NbExp=3; IntAct=EBI-747133, EBI-12175871;
CC       P27658; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-747133, EBI-10251462;
CC       P27658; O43257: ZNHIT1; NbExp=3; IntAct=EBI-747133, EBI-347522;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- TISSUE SPECIFICITY: Expressed primarily in the subendothelium of large
CC       blood vessels. Also expressed in arterioles and venules in muscle,
CC       heart, kidney, spleen, umbilical cord, liver and lung and is also found
CC       in connective tissue layers around hair follicles, around nerve bundles
CC       in muscle, in the dura of the optic nerve, in cornea and sclera, and in
CC       the perichondrium of cartilaginous tissues. In the kidney, expressed in
CC       mesangial cells, glomerular endothelial cells, and tubular epithelial
CC       cells. Also expressed in mast cells, and in astrocytes during the
CC       repair process. Expressed in Descemet's membrane. Specifically
CC       expressed in peritoneal fibroblasts and mesothelial cells.
CC       {ECO:0000269|PubMed:10686422, ECO:0000269|PubMed:2376131,
CC       ECO:0000269|PubMed:7734329}.
CC   -!- INDUCTION: Up-regulated during vascular injury, in atherosclerosis and
CC       in diabetes. {ECO:0000269|PubMed:17888087}.
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: Proteolytically cleaved by neutrophil elastase, in vitro.
CC       Proteolytic processing produces the C-terminal NC1 domain fragment,
CC       vastatin. {ECO:0000269|PubMed:1515454}.
CC   -!- MISCELLANEOUS: Four consecutive Gly-Pro-Pro triplets are present at the
CC       C-terminus of the triple-helical region. These may provide the high
CC       thermal stability of this region.
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DR   EMBL; X57527; CAA40748.1; -; mRNA.
DR   EMBL; BT009917; AAP88919.1; -; mRNA.
DR   EMBL; CH471052; EAW79837.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79838.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW79840.1; -; Genomic_DNA.
DR   EMBL; BC013581; AAH13581.1; -; mRNA.
DR   CCDS; CCDS2934.1; -.
DR   PIR; S15435; S15435.
DR   RefSeq; NP_001841.2; NM_001850.4.
DR   RefSeq; NP_065084.2; NM_020351.3.
DR   AlphaFoldDB; P27658; -.
DR   SMR; P27658; -.
DR   BioGRID; 107692; 130.
DR   ComplexPortal; CPX-1745; Collagen type VIII trimer variant 1.
DR   ComplexPortal; CPX-1746; Collagen type VIII trimer variant 2.
DR   IntAct; P27658; 72.
DR   MINT; P27658; -.
DR   STRING; 9606.ENSP00000261037; -.
DR   GlyCosmos; P27658; 1 site, 1 glycan.
DR   GlyGen; P27658; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P27658; -.
DR   PhosphoSitePlus; P27658; -.
DR   BioMuta; COL8A1; -.
DR   DMDM; 21903375; -.
DR   EPD; P27658; -.
DR   jPOST; P27658; -.
DR   MassIVE; P27658; -.
DR   PaxDb; 9606-ENSP00000261037; -.
DR   PeptideAtlas; P27658; -.
DR   ProteomicsDB; 54404; -.
DR   Pumba; P27658; -.
DR   Antibodypedia; 32194; 215 antibodies from 28 providers.
DR   DNASU; 1295; -.
DR   Ensembl; ENST00000261037.7; ENSP00000261037.3; ENSG00000144810.16.
DR   Ensembl; ENST00000273342.8; ENSP00000273342.3; ENSG00000144810.16.
DR   Ensembl; ENST00000652472.1; ENSP00000498483.1; ENSG00000144810.16.
DR   GeneID; 1295; -.
DR   KEGG; hsa:1295; -.
DR   MANE-Select; ENST00000652472.1; ENSP00000498483.1; NM_020351.4; NP_065084.2.
DR   UCSC; uc003dtg.3; human.
DR   AGR; HGNC:2215; -.
DR   CTD; 1295; -.
DR   DisGeNET; 1295; -.
DR   GeneCards; COL8A1; -.
DR   HGNC; HGNC:2215; COL8A1.
DR   HPA; ENSG00000144810; Low tissue specificity.
DR   MIM; 120251; gene.
DR   neXtProt; NX_P27658; -.
DR   OpenTargets; ENSG00000144810; -.
DR   PharmGKB; PA26731; -.
DR   VEuPathDB; HostDB:ENSG00000144810; -.
DR   eggNOG; ENOG502QRFR; Eukaryota.
DR   GeneTree; ENSGT00940000158272; -.
DR   HOGENOM; CLU_001074_21_0_1; -.
DR   InParanoid; P27658; -.
DR   OMA; PMGKEMP; -.
DR   OrthoDB; 5267071at2759; -.
DR   PhylomeDB; P27658; -.
DR   TreeFam; TF334029; -.
DR   PathwayCommons; P27658; -.
DR   Reactome; R-HSA-1442490; Collagen degradation.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
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-8948216; Collagen chain trimerization.
DR   SignaLink; P27658; -.
DR   BioGRID-ORCS; 1295; 14 hits in 1139 CRISPR screens.
DR   ChiTaRS; COL8A1; human.
DR   GeneWiki; Collagen,_type_VIII,_alpha_1; -.
DR   GenomeRNAi; 1295; -.
DR   Pharos; P27658; Tbio.
DR   PRO; PR:P27658; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P27658; Protein.
DR   Bgee; ENSG00000144810; Expressed in visceral pleura and 157 other cell types or tissues.
DR   ExpressionAtlas; P27658; baseline and differential.
DR   GO; GO:0005591; C:collagen type VIII trimer; TAS:ProtInc.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
DR   GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR   Gene3D; 2.60.120.40; -; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR15427:SF33; EMI DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS50871; C1Q; 1.
DR   Genevisible; P27658; HS.
PE   1: Evidence at protein level;
KW   Angiogenesis; Basement membrane; Cell adhesion; Collagen;
KW   Extracellular matrix; Hydroxylation; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..744
FT                   /note="Collagen alpha-1(VIII) chain"
FT                   /id="PRO_0000005762"
FT   CHAIN           572..744
FT                   /note="Vastatin"
FT                   /id="PRO_0000390484"
FT   DOMAIN          611..744
FT                   /note="C1q"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00368"
FT   REGION          29..117
FT                   /note="Nonhelical region (NC2)"
FT   REGION          115..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..571
FT                   /note="Triple-helical region (COL1)"
FT   REGION          459..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..744
FT                   /note="Nonhelical region (NC1)"
FT   COMPBIAS        125..139
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..217
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..269
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..307
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..531
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..583
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        262
FT                   /note="P -> L (in Ref. 1; CAA40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="P -> R (in Ref. 1; CAA40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="P -> A (in Ref. 1; CAA40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="A -> S (in Ref. 1; CAA40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        388
FT                   /note="P -> S (in Ref. 1; CAA40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        454
FT                   /note="L -> F (in Ref. 1; CAA40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="A -> H (in Ref. 1; CAA40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        601
FT                   /note="Y -> T (in Ref. 1; CAA40748)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        631
FT                   /note="A -> G (in Ref. 1; CAA40748)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   744 AA;  73364 MW;  2BC1B0955DE2C9A3 CRC64;
     MAVLPGPLQL LGVLLTISLS SIRLIQAGAY YGIKPLPPQI PPQMPPQIPQ YQPLGQQVPH
     MPLAKDGLAM GKEMPHLQYG KEYPHLPQYM KEIQPAPRMG KEAVPKKGKE IPLASLRGEQ
     GPRGEPGPRG PPGPPGLPGH GIPGIKGKPG PQGYPGVGKP GMPGMPGKPG AMGMPGAKGE
     IGQKGEIGPM GIPGPQGPPG PHGLPGIGKP GGPGLPGQPG PKGDRGPKGL PGPQGLRGPK
     GDKGFGMPGA PGVKGPPGMH GPPGPVGLPG VGKPGVTGFP GPQGPLGKPG APGEPGPQGP
     IGVPGVQGPP GIPGIGKPGQ DGIPGQPGFP GGKGEQGLPG LPGPPGLPGI GKPGFPGPKG
     DRGMGGVPGA LGPRGEKGPI GAPGIGGPPG EPGLPGIPGP MGPPGAIGFP GPKGEGGIVG
     PQGPPGPKGE PGLQGFPGKP GFLGEVGPPG MRGLPGPIGP KGEAGQKGVP GLPGVPGLLG
     PKGEPGIPGD QGLQGPPGIP GIGGPSGPIG PPGIPGPKGE PGLPGPPGFP GIGKPGVAGL
     HGPPGKPGAL GPQGQPGLPG PPGPPGPPGP PAVMPPTPPP QGEYLPDMGL GIDGVKPPHA
     YGAKKGKNGG PAYEMPAFTA ELTAPFPPVG APVKFNKLLY NGRQNYNPQT GIFTCEVPGV
     YYFAYHVHCK GGNVWVALFK NNEPVMYTYD EYKKGFLDQA SGSAVLLLRP GDRVFLQMPS
     EQAAGLYAGQ YVHSSFSGYL LYPM
//