LAMC1_XENTR
ID LAMC1_XENTR Reviewed; 1592 AA.
AC A0JP86;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Laminin subunit gamma-1;
DE Flags: Precursor;
GN Name=lamc1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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. {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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250}.
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DR EMBL; BC127297; AAI27298.1; -; mRNA.
DR RefSeq; NP_001090659.1; NM_001097190.1.
DR AlphaFoldDB; A0JP86; -.
DR SMR; A0JP86; -.
DR PaxDb; A0JP86; -.
DR PRIDE; A0JP86; -.
DR DNASU; 100036631; -.
DR GeneID; 100036631; -.
DR KEGG; xtr:100036631; -.
DR CTD; 3915; -.
DR Xenbase; XB-GENE-478553; lamc1.
DR eggNOG; KOG1836; Eukaryota.
DR InParanoid; A0JP86; -.
DR OrthoDB; 156553at2759; -.
DR Reactome; R-XTR-3000157; Laminin interactions.
DR Reactome; R-XTR-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-XTR-8874081; MET activates PTK2 signaling.
DR Reactome; R-XTR-8957275; Post-translational protein phosphorylation.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 10.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 11.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 11.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01248; EGF_LAM_1; 10.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 2: Evidence at transcript level;
KW Basement membrane; Cell adhesion; Coiled coil; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1592
FT /note="Laminin subunit gamma-1"
FT /id="PRO_0000364202"
FT DOMAIN 29..268
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 269..324
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 325..380
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 381..427
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 428..477
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 504..672
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 707..755
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 756..810
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 811..866
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 867..917
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 918..965
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 966..1013
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1013..1592
FT /note="Domain II and I"
FT /evidence="ECO:0000250"
FT REGION 1456..1489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1018..1477
FT /evidence="ECO:0000255"
FT COILED 1515..1579
FT /evidence="ECO:0000255"
FT COMPBIAS 1457..1476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1005
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 1048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 269..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 271..288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 290..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 302..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 325..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 327..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 353..362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 365..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 381..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 383..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 401..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 413..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 428..439
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 430..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 448..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 460..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 707..716
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 709..723
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 725..734
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 737..753
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 756..764
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 758..775
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 778..787
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 790..808
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 811..825
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 813..832
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 835..844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 847..864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 867..881
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 869..888
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 890..899
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 902..915
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 918..930
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 920..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 939..948
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 951..963
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 966..978
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 968..984
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 986..995
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 998..1011
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1592 AA; 175580 MW; 458E53775436C3CA CRC64;
MRAPVLAVLA VLLLGTVRAA MDECYEEGSP QRCMPEFVNA AFNATVVATN TCGTPPEEYC
VQTGVTGVTK SCHICDSGQF HLQHGAEYLT DYNNQAEITW WQSQTMLAGI QYPSTINLTL
HLGKAFDITY VRLKFHTSRP ESFALYKRTH EDGPWIPYQY YSGSCEKTYQ KFNRGFIRTG
EDEQQALCTD EFSDISPLTG GNVAFSTLEG RPSAYNFDNS PVLQEWVTAT DIRVTLNRLN
TFGDEVFSDP KVLKSYYYAI SDFAVGGRCK CNGHASECVR NEFEKIVCNC KHNTFGSDCE
KCLPFYNDRP WRRSTADSPN ECLPCNCNGR SQECYFDPEL YRSTGHGGHC TGCADNTDGP
NCERCRENYY RQDNNEPCHA CQCNPVGSLS TQCDNYGRCS CKPGVMGEKC DRCQPGFHSL
TEAGCRPCAC NPAGSTDECN VETGRCSCKD NVEGFNCERC KPGFFHLDEA NPRGCTPCFC
YGHSSVCSSA EGYRVSSIVS TFESGVEGWT AQQRDGSEYS LSWVSDSSAV SVISESYFPI
YFIAPAKFLG NQGASYGQNL TFSFRVERRD TRLSAEDLVL EGAGLRVSVP LIAQGNSYPS
ETTQRYIFRM HEATDYPWRP SVSPFEFQKM LQNLTAIKIR GSYSERSAGF LEEVSLVTAV
AGAGPSAPWV EICSCPTGYI GQFCERCAPG YRRENPSQGP YSPCVLCTCN GHSDTCDPES
GVCDCQHNTA GPHCERCSEG YYGDSTTGSA SDCQPCPCPG GSSCAVVPRT KEVVCTNCPL
GTTGKRCELC DDGYFGDPLG ENGAPRPCRI CECSNNIDPN AVGNCDRLTG ECLKCIYNTG
GFYCDRCRDG FYGNPLAQNP DLKCRACSCN PYGTVKGQSG CNQVTGQCEC LPHVTERDCS
ACEPGFYNLL SGRGCERCDC HSLGSTSGQC DVRTGQCECH PGISGQQCQQ CEPNHFGFGP
EGCKPCDCDP EGSGSLQCKE DGRCECKSGF VGTRCDQCEE NYFYNRSGPG CQECPACYRL
VKDKVNEQRG KLQELEDLLK NLSTGEENIT DQAFEERLRE AEKAVNDLLL DAQSSKDVDQ
GMLDRLAEIN TTLSFQLERL QNIRDMIRDT DKQAQEARDR VENTEFIIDS ARVQLEKAKM
AIANVSITPP ESTGDPNNMT LLAEEARKLA ERHMQEARDI EKAAKEANDT ANEALRLLQK
TLASENQTAL DIEELNRKYA QAKDIARELE KQASKVHAEA EEAGNRALQI YANLTSVPSI
DTTALQNEAD KIQKEAEELD SLIDRKLRDY EDLREDMRGR EMEVKNLLDK GKTEQQTADQ
LLARADAAKA QAEEAAKKGR ETLQEANDIL NKLRDFDKRV NDNKTAAEAA LRKIPMIAQT
IAEANNKTRQ AESALGNANA DARGAKSKAE EAEALANTVQ KKAATARAEA DNTFKEVTDL
DGELQDMLQQ LQEAENQLKK KQAEAESDEK MAEMASNATK DAESNANNSK KSVNGVLATI
DELLSRLGQL DSVDVGQLTV LEKTLDDAKN QLRDSDLDRK LAELQESSNL QRVALDSYSR
DIDQILRDIA NLEDIKNTLP AGCYNTPIIE KP
