LAMB1_MOUSE
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 03-AUG-2022, entry version 203.
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 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 [6]
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 [7]
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 [8]
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). {ECO:0000250}.
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), laminin-2 (laminin-
CC 211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8
CC (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213)
CC (By similarity). Interacts with ITGB1 (PubMed:34427057).
CC {ECO:0000250|UniProtKB:Q01635, ECO:0000269|PubMed:34427057}.
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};
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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; XP_006515055.2; XM_006514992.3.
DR RefSeq; XP_006515056.1; XM_006514993.1.
DR PDB; 4AQS; X-ray; 3.11 A; A=22-542.
DR PDB; 5MC9; X-ray; 2.13 A; B=1735-1786.
DR PDBsum; 4AQS; -.
DR PDBsum; 5MC9; -.
DR AlphaFoldDB; P02469; -.
DR BMRB; P02469; -.
DR SMR; P02469; -.
DR BioGRID; 201101; 12.
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 IntAct; P02469; 11.
DR MINT; P02469; -.
DR STRING; 10090.ENSMUSP00000002979; -.
DR GlyConnect; 2459; 2 N-Linked glycans (2 sites).
DR GlyGen; P02469; 13 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; P02469; -.
DR PhosphoSitePlus; P02469; -.
DR jPOST; P02469; -.
DR MaxQB; P02469; -.
DR PaxDb; P02469; -.
DR PeptideAtlas; P02469; -.
DR PRIDE; P02469; -.
DR ProteomicsDB; 264911; -.
DR Antibodypedia; 1361; 453 antibodies from 42 providers.
DR DNASU; 16777; -.
DR Ensembl; ENSMUST00000002979; ENSMUSP00000002979; ENSMUSG00000002900.
DR Ensembl; ENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900.
DR GeneID; 16777; -.
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 Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 16777; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Lamb1; mouse.
DR PRO; PR:P02469; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P02469; protein.
DR Bgee; ENSMUSG00000002900; Expressed in metanephric loop of Henle and 321 other tissues.
DR ExpressionAtlas; P02469; baseline and differential.
DR Genevisible; P02469; MM.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043256; C:laminin complex; IDA:MGI.
DR GO; GO:0005606; C:laminin-1 complex; IDA:MGI.
DR GO; GO:0043259; C:laminin-10 complex; IPI:MGI.
DR GO; GO:0005607; C:laminin-2 complex; ISS:HGNC-UCL.
DR GO; GO:0043257; C:laminin-8 complex; ISS:HGNC-UCL.
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; IC: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:0009887; P:animal organ morphogenesis; 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: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:MGI.
DR GO; GO:0042476; P:odontogenesis; ISS:HGNC-UCL.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IC: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; IC:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IC:ComplexPortal.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC:ComplexPortal.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 13.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
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.
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 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..172
FT /evidence="ECO:0007829|PDB:4AQS"
FT STRAND 173..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 STRAND 304..309
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
