ID LAMB1_MOUSE Reviewed; 1786 AA. AC P02469; E9PXZ9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 02-SEP-2026, entry version 222. DE RecName: Full=Laminin subunit beta-1; DE AltName: Full=Laminin B1 chain; DE AltName: Full=Laminin-1 subunit beta; DE AltName: Full=Laminin-10 subunit beta; DE AltName: Full=Laminin-12 subunit beta; DE AltName: Full=Laminin-2 subunit beta; DE AltName: Full=Laminin-6 subunit beta; DE AltName: Full=Laminin-8 subunit beta; DE Flags: Precursor; GN Name=Lamb1; Synonyms=Lamb-1, Lamb1-1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3493487; DOI=10.1073/pnas.84.4.935; RA Sasaki M., Kato S., Kohno K., Martin G.R., Yamada Y.; RT "Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain RT protein containing cysteine-rich repeats."; RL Proc. Natl. Acad. Sci. U.S.A. 84:935-939(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1292-1786. RX PubMed=6209134; DOI=10.1002/j.1460-2075.1984.tb02140.x; RA Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.; RT "Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled- RT coil alpha-helix."; RL EMBO J. 3:2355-2362(1984). RN [4] RP PROTEIN SEQUENCE OF 165-172; 539-547 AND 712-719. RC STRAIN=BALB/cJ; TISSUE=Endothelial cell; RX PubMed=9219532; DOI=10.1111/j.1432-1033.1997.t01-1-00727.x; RA Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R., RA Sorokin L.M.; RT "Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of RT endothelium."; RL Eur. J. Biochem. 246:727-735(1997). RN [5] RP FUNCTION, AND SUBUNIT. RX PubMed=9454835; DOI=10.1523/jneurosci.18-04-01250.1998; RA Montanaro F., Gee S.H., Jacobson C., Lindenbaum M.H., Froehner S.C., RA Carbonetto S.; RT "Laminin and alpha-dystroglycan mediate acetylcholine receptor aggregation RT via a MuSK-independent pathway."; RL J. Neurosci. 18:1250-1260(1998). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279; ASN-1336 AND ASN-1343. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and RC Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP TISSUE SPECIFICITY. RX PubMed=23472759; DOI=10.1016/j.ajhg.2013.02.005; RA Radmanesh F., Caglayan A.O., Silhavy J.L., Yilmaz C., Cantagrel V., RA Omar T., Rosti B., Kaymakcalan H., Gabriel S., Li M., Sestan N., RA Bilguvar K., Dobyns W.B., Zaki M.S., Gunel M., Gleeson J.G.; RT "Mutations in LAMB1 cause cobblestone brain malformation without muscular RT or ocular abnormalities."; RL Am. J. Hum. Genet. 92:468-474(2013). RN [9] RP INTERACTION WITH ITGB1. RX PubMed=34427057; DOI=10.1002/jcsm.12767; RA Luo W., Lin Z., Chen J., Chen G., Zhang S., Liu M., Li H., He D., Liang S., RA Luo Q., Zhang D., Nie Q., Zhang X.; RT "TMEM182 interacts with integrin beta 1 and regulates myoblast RT differentiation and muscle regeneration."; RL J. Cachexia Sarcopenia Muscle 12:1704-1723(2021). CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is CC thought to mediate the attachment, migration and organization of cells CC into tissues during embryonic development by interacting with other CC extracellular matrix components. Involved in the organization of the CC laminar architecture of the cerebral cortex (By similarity). It is CC probably required for the integrity of the basement membrane/glia CC limitans that serves as an anchor point for the endfeet of radial glial CC cells and as a physical barrier to migrating neurons (By similarity). CC Radial glial cells play a central role in cerebral cortical CC development, where they act both as the proliferative unit of the CC cerebral cortex and a scaffold for neurons migrating toward the pial CC surface (By similarity). As a subunit of laminin-1 (also known as CC laminin-111 or EHS laminin), it is involved in the stimulation of CC agrin-induced receptor clustering through a MuSK-independent pathway CC (PubMed:9454835). {ECO:0000250, ECO:0000269|PubMed:9454835}. CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three CC different polypeptide chains (alpha, beta, gamma), which are bound to CC each other by disulfide bonds into a cross-shaped molecule comprising CC one long and three short arms with globules at each end. Beta-1 is a CC subunit of laminin-1 (laminin-111 or EHS laminin) (PubMed:9454835). CC Beta-1 is also a subunit of laminin-2 (laminin-211 or merosin), CC laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin- CC 10 (laminin-511) and laminin-12 (laminin-213) (By similarity). CC Interacts with ITGB1 (PubMed:34427057). {ECO:0000250|UniProtKB:Q01635, CC ECO:0000269|PubMed:34427057, ECO:0000269|PubMed:9454835}. CC -!- INTERACTION: CC P02469; P02468: Lamc1; NbExp=4; IntAct=EBI-6662997, EBI-7059830; CC P02469; P31696: AGRN; Xeno; NbExp=2; IntAct=EBI-6662997, EBI-457650; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. Note=Major component. CC -!- TISSUE SPECIFICITY: Widely expressed in the embryo. High levels are CC detected in the cerebellar basement membrane, at postnatal day 7. CC {ECO:0000269|PubMed:23472759}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA39407.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; M15525; AAA39407.1; ALT_INIT; mRNA. DR EMBL; CR974423; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CT571245; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X05212; CAA28839.1; -; mRNA. DR CCDS; CCDS25862.2; -. DR PIR; A26413; MMMSB1. DR RefSeq; NP_032508.3; NM_008482.3. DR RefSeq; XP_006515056.1; XM_006514993.2. DR PDB; 4AQS; X-ray; 3.11 A; A=22-542. DR PDB; 5MC9; X-ray; 2.13 A; B=1735-1786. DR AlphaFoldDB; P02469; -. DR BMRB; P02469; -. DR SMR; P02469; -. DR BioGRID; 201101; 13. DR ComplexPortal; CPX-3008; Laminin-111 complex. DR ComplexPortal; CPX-3009; Laminin-211 complex. DR ComplexPortal; CPX-3013; Laminin-311 complex variant A. DR ComplexPortal; CPX-3015; Laminin-411 complex. DR ComplexPortal; CPX-3016; Laminin-511 complex. DR ComplexPortal; CPX-3018; Laminin-213 complex. DR ComplexPortal; CPX-3167; Laminin-311 complex variant B. DR FunCoup; P02469; 896. DR IntAct; P02469; 12. DR MINT; P02469; -. DR STRING; 10090.ENSMUSP00000002979; -. DR GlyConnect; P02469; 2 N-Linked glycans (2 sites). DR GlyCosmos; P02469; 12 sites, 2 glycans. DR GlyGen; P02469; 14 sites, 9 N-linked glycans (7 sites), 1 O-linked glycan (1 site). DR iPTMnet; P02469; -. DR MetOSite; P02469; -. DR PhosphoSitePlus; P02469; -. DR jPOST; P02469; -. DR PaxDb; 10090-ENSMUSP00000002979; -. DR PeptideAtlas; P02469; -. DR ProteomicsDB; 264911; -. DR Pumba; P02469; -. DR Antibodypedia; 1361; 443 antibodies from 43 providers. DR DNASU; 16777; -. DR Ensembl; ENSMUST00000002979.16; ENSMUSP00000002979.10; ENSMUSG00000002900.18. DR Ensembl; ENSMUST00000169088.8; ENSMUSP00000132778.2; ENSMUSG00000002900.18. DR GeneID; 16777; -. DR KEGG; mmu:16777; -. DR AGR; MGI:96743; -. DR CTD; 3912; -. DR MGI; MGI:96743; Lamb1. DR VEuPathDB; HostDB:ENSMUSG00000002900; -. DR eggNOG; KOG0994; Eukaryota. DR GeneTree; ENSGT00940000156003; -. DR HOGENOM; CLU_001560_1_0_1; -. DR InParanoid; P02469; -. DR OrthoDB; 5985440at2759; -. DR BioGRID-ORCS; 16777; 1 hit in 62 CRISPR screens. DR EvolutionaryTrace; P02469; -. DR PRO; PR:P02469; -. DR Proteomes; UP000000589; Chromosome 12. DR RNAct; P02469; protein. DR Bgee; ENSMUSG00000002900; Expressed in metanephric loop of Henle and 325 other cell types or tissues. DR ExpressionAtlas; P02469; baseline and differential. DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB. DR GO; GO:0031012; C:extracellular matrix; IDA:MGI. DR GO; GO:0005576; C:extracellular region; ISO:GO_Central. DR GO; GO:0043256; C:laminin trimer; IDA:MGI. DR GO; GO:0005606; C:laminin-111 trimer; IDA:UniProtKB. DR GO; GO:0005607; C:laminin-211 trimer; ISS:HGNC-UCL. DR GO; GO:0043261; C:laminin-213 trimer; TAS:GO_Central. DR GO; GO:0005611; C:laminin-311 trimer; TAS:GO_Central. DR GO; GO:0043257; C:laminin-411 trimer; ISS:HGNC-UCL. DR GO; GO:0043259; C:laminin-511 trimer; IPI:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; NAS:ComplexPortal. DR GO; GO:0019899; F:enzyme binding; IPI:MGI. DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:HGNC-UCL. DR GO; GO:0043208; F:glycosphingolipid binding; IDA:MGI. DR GO; GO:0005178; F:integrin binding; IMP:MGI. DR GO; GO:0048018; F:receptor ligand activity; IMP:UniProtKB. DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central. DR GO; GO:0007411; P:axon guidance; IBA:GO_Central. DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central. DR GO; GO:0016477; P:cell migration; IMP:MGI. DR GO; GO:0007566; P:embryo implantation; IMP:MGI. DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl. DR GO; GO:0007611; P:learning or memory; NAS:UniProtKB. DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB. DR GO; GO:0031175; P:neuron projection development; IDA:MGI. DR GO; GO:0021812; P:neuronal-glial interaction involved in cerebral cortex radial glia guided migration; ISO:GO_Central. DR GO; GO:0042476; P:odontogenesis; ISS:HGNC-UCL. DR GO; GO:0045785; P:positive regulation of cell adhesion; NAS:ComplexPortal. DR GO; GO:0030335; P:positive regulation of cell migration; ISS:HGNC-UCL. DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; NAS:ComplexPortal. DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; NAS:ComplexPortal. DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; IDA:UniProtKB. DR GO; GO:0110011; P:regulation of basement membrane organization; NAS:ComplexPortal. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:GO_Central. DR GO; GO:0009888; P:tissue development; IBA:GO_Central. DR CDD; cd22300; cc_LAMB1_C; 1. DR CDD; cd00055; EGF_Lam; 13. DR DisProt; DP02810; -. DR FunFam; 2.10.25.10:FF:000011; Cadherin EGF LAG seven-pass G-type receptor; 1. DR FunFam; 2.10.25.10:FF:000083; Laminin subunit alpha; 1. DR FunFam; 2.10.25.10:FF:000084; Laminin subunit alpha 3; 1. DR FunFam; 2.10.25.10:FF:000065; Laminin subunit beta 1; 1. DR FunFam; 2.10.25.10:FF:000101; Laminin subunit beta 1; 1. DR FunFam; 2.10.25.10:FF:000130; Laminin subunit beta 1; 1. DR FunFam; 2.10.25.10:FF:000138; Laminin subunit beta 1; 1. DR FunFam; 2.10.25.10:FF:000145; Laminin subunit beta 1; 1. DR FunFam; 2.170.300.10:FF:000004; Laminin subunit beta 1; 1. DR FunFam; 2.60.120.260:FF:000010; Laminin subunit beta 1; 1. DR FunFam; 2.10.25.10:FF:000135; Laminin subunit beta 4; 2. DR FunFam; 2.10.25.10:FF:000280; Laminin subunit beta 4; 1. DR FunFam; 2.170.300.10:FF:000001; Laminin subunit beta-1; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.10.25.10; Laminin; 9. DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2. DR InterPro; IPR000742; EGF. DR InterPro; IPR056558; LAMB1-4_helical. DR InterPro; IPR050440; Laminin/Netrin_ECM. DR InterPro; IPR013015; Laminin_IV_B. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR002049; LE_dom. DR InterPro; IPR056863; LMN_ATRN_NET-like_EGF. DR PANTHER; PTHR10574:SF233; LAMININ SUBUNIT BETA-1; 1. DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1. DR Pfam; PF00053; EGF_laminin; 11. DR Pfam; PF24973; EGF_LMN_ATRN; 2. DR Pfam; PF23219; LAMB1; 1. DR Pfam; PF21199; LAMININ_IV_B; 1. DR Pfam; PF00055; Laminin_N; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00181; EGF; 10. DR SMART; SM00180; EGF_Lam; 13. DR SMART; SM00136; LamNT; 1. DR SUPFAM; SSF57196; EGF/Laminin; 13. DR PROSITE; PS00022; EGF_1; 9. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS01248; EGF_LAM_1; 11. DR PROSITE; PS50027; EGF_LAM_2; 13. DR PROSITE; PS51116; LAMININ_IVB; 1. DR PROSITE; PS51117; LAMININ_NTER; 1. DR PDBsum; 4AQS; -. DR PDBsum; 5MC9; -. PE 1: Evidence at protein level; KW 3D-structure; Basement membrane; Cell adhesion; Coiled coil; KW Direct protein sequencing; Disulfide bond; Extracellular matrix; KW Glycoprotein; Laminin EGF-like domain; Phosphoprotein; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1..21 FT CHAIN 22..1786 FT /note="Laminin subunit beta-1" FT /id="PRO_0000017066" FT DOMAIN 31..270 FT /note="Laminin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466" FT DOMAIN 271..334 FT /note="Laminin EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 335..397 FT /note="Laminin EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 398..457 FT /note="Laminin EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 458..509 FT /note="Laminin EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 510..540 FT /note="Laminin EGF-like 5; truncated" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 549..767 FT /note="Laminin IV type B" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00462" FT DOMAIN 773..820 FT /note="Laminin EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 821..866 FT /note="Laminin EGF-like 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 867..916 FT /note="Laminin EGF-like 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 917..975 FT /note="Laminin EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 976..1027 FT /note="Laminin EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1028..1083 FT /note="Laminin EGF-like 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1084..1131 FT /note="Laminin EGF-like 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DOMAIN 1132..1178 FT /note="Laminin EGF-like 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT REGION 1179..1397 FT /note="Domain II" FT REGION 1398..1430 FT /note="Domain alpha" FT REGION 1431..1786 FT /note="Domain I" FT COILED 1216..1315 FT /evidence="ECO:0000255" FT COILED 1368..1388 FT /evidence="ECO:0000255" FT COILED 1448..1778 FT /evidence="ECO:0000255" FT MOD_RES 250 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1496 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07942" FT MOD_RES 1666 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P07942" FT CARBOHYD 120 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 356 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 519 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 677 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1041 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1195 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1279 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 1336 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 1343 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 1487 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1542 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1643 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 271..280 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 273..298 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 300..309 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 312..332 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 335..344 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 337..362 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 365..374 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 377..395 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 398..411 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 400..426 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 428..437 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 440..455 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 458..472 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 460..479 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 481..490 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 493..507 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 510..522 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 512..529 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 531..540 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 773..785 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 775..792 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 794..803 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 806..818 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 821..833 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 823..840 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 842..851 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 854..864 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 867..876 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 869..883 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 886..895 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 898..914 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 917..933 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 919..944 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 946..955 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 958..973 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 976..990 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 978..997 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1000..1009 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1012..1025 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1028..1040 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1030..1054 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1056..1065 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1068..1081 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1084..1096 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1086..1103 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1105..1114 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1117..1129 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1132..1144 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1134..1151 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1153..1162 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1165..1176 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460" FT DISULFID 1179 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1182 FT /note="Interchain" FT /evidence="ECO:0000305" FT DISULFID 1785 FT /note="Interchain" FT /evidence="ECO:0000305" FT CONFLICT 159 FT /note="A -> T (in Ref. 1; AAA39407)" FT /evidence="ECO:0000305" FT CONFLICT 569 FT /note="I -> V (in Ref. 1; AAA39407)" FT /evidence="ECO:0000305" FT CONFLICT 993 FT /note="E -> D (in Ref. 1; AAA39407)" FT /evidence="ECO:0000305" FT CONFLICT 1393 FT /note="V -> A (in Ref. 1; AAA39407 and 3; CAA28839)" FT /evidence="ECO:0000305" FT CONFLICT 1531..1534 FT /note="MEMP -> SGNA (in Ref. 1; AAA39407)" FT /evidence="ECO:0000305" FT CONFLICT 1692 FT /note="G -> C (in Ref. 3; CAA28839)" FT /evidence="ECO:0000305" FT CONFLICT 1749 FT /note="D -> N (in Ref. 3; CAA28839)" FT /evidence="ECO:0000305" FT HELIX 30..32 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 40..43 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 69..72 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:4AQS" FT TURN 87..89 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 122..142 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 146..155 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 161..169 FT /evidence="ECO:0007829|PDB:4AQS" FT TURN 170..173 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 174..177 FT /evidence="ECO:0007829|PDB:4AQS" FT TURN 200..202 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 204..210 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 212..214 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 222..228 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 229..239 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 252..255 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 261..270 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 293..295 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 304..309 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 331..335 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 342..346 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 348..353 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 360..364 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 381..383 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 395..397 FT /evidence="ECO:0007829|PDB:4AQS" FT TURN 402..404 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 407..409 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 417..419 FT /evidence="ECO:0007829|PDB:4AQS" FT TURN 434..437 FT /evidence="ECO:0007829|PDB:4AQS" FT STRAND 454..457 FT /evidence="ECO:0007829|PDB:4AQS" FT TURN 462..464 FT /evidence="ECO:0007829|PDB:4AQS" FT TURN 474..476 FT /evidence="ECO:0007829|PDB:4AQS" FT TURN 488..490 FT /evidence="ECO:0007829|PDB:4AQS" FT HELIX 1739..1784 FT /evidence="ECO:0007829|PDB:5MC9" SQ SEQUENCE 1786 AA; 197090 MW; E7F258170C3626DD CRC64; MGLLQVFAFG VLALWGTRVC AQEPEFSYGC AEGSCYPATG DLLIGRAQKL SVTSTCGLHK PEPYCIVSHL QEDKKCFICD SRDPYHETLN PDSHLIENVV TTFAPNRLKI WWQSENGVEN VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI ERSSDFGKAW GVYRYFAYDC ESSFPGISTG PMKKVDDIIC DSRYSDIEPS TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL HTLGDNLLDS RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGVNEEV EGMVHGHCMC RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SSSCHFDMAV FLATGNVSGG VCDNCQHNTM GRNCEQCKPF YFQHPERDIR DPNLCEPCTC DPAGSENGGI CDGYTDFSVG LIAGQCRCKL HVEGERCDVC KEGFYDLSAE DPYGCKSCAC NPLGTIPGGN PCDSETGYCY CKRLVTGQRC DQCLPQHWGL SNDLDGCRPC DCDLGGALNN SCSEDSGQCS CLPHMIGRQC NEVESGYYFT TLDHYIYEAE EANLGPGVIV VERQYIQDRI PSWTGPGFVR VPEGAYLEFF IDNIPYSMEY EILIRYEPQL PDHWEKAVIT VQRPGKIPAS SRCGNTVPDD DNQVVSLSPG SRYVVLPRPV CFEKGMNYTV RLELPQYTAS GSDVESPYTF IDSLVLMPYC KSLDIFTVGG SGDGEVTNSA WETFQRYRCL ENSRSVVKTP MTDVCRNIIF SISALIHQTG LACECDPQGS LSSVCDPNGG QCQCRPNVVG RTCNRCAPGT FGFGPNGCKP CDCHLQGSAS AFCDAITGQC HCFQGIYARQ CDRCLPGYWG FPSCQPCQCN GHALDCDTVT GECLSCQDYT TGHNCERCLA GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY IGSRCDDCAS GFFGNPSDFG GSCQPCQCHH NIDTTDPEAC DKETGRCLKC LYHTEGDHCQ LCQYGYYGDA LRQDCRKCVC NYLGTVKEHC NGSDCHCDKA TGQCSCLPNV IGQNCDRCAP NTWQLASGTG CGPCNCNAAH SFGPSCNEFT GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE TPQCDQSTGQ CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDAII GELTNRTHKF LEKAKALKIS GVIGPYRETV DSVEKKVNEI KDILAQSPAA EPLKNIGILF EEAEKLTKDV TEKMAQVEVK LTDTASQSNS TAGELGALQA EAESLDKTVK ELAEQLEFIK NSDIQGALDS ITKYFQMSLE AEKRVNASTT DPNSTVEQSA LTRDRVEDLM LERESPFKEQ QEEQARLLDE LAGKLQSLDL SAVAQMTCGT PPGADCSESE CGGPNCRTDE GEKKCGGPGC GGLVTVAHSA WQKAMDFDRD VLSALAEVEQ LSKMVSEAKV RADEAKQNAQ DVLLKTNATK EKVDKSNEDL RNLIKQIRNF LTEDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER VETLSQVEVI LQQSAADIAR AELLLEEAKR ASKSATDVKV TADMVKEALE EAEKAQVAAE KAIKQADEDI QGTQNLLTSI ESETAASEET LTNASQRISK LERNVEELKR KAAQNSGEAE YIEKVVYSVK QNADDVKKTL DGELDEKYKK VESLIAQKTE ESADARRKAE LLQNEAKTLL AQANSKLQLL EDLERKYEDN QKYLEDKAQE LVRLEGEVRS LLKDISEKVA VYSTCL //