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Protein

Laminin subunit gamma-1

Gene

lamc1

Organism
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-1
Gene namesi
Name:lamc1
OrganismiXenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Taxonomic identifieri8364 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusSilurana
Proteomesi
  • UP000008143 Componenti: Unassembled WGS sequence

Organism-specific databases

XenbaseiXB-GENE-478553. lamc1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 15921573Laminin subunit gamma-1PRO_0000364202Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi269 ↔ 278PROSITE-ProRule annotation
Disulfide bondi271 ↔ 288PROSITE-ProRule annotation
Disulfide bondi290 ↔ 299PROSITE-ProRule annotation
Disulfide bondi302 ↔ 322PROSITE-ProRule annotation
Disulfide bondi325 ↔ 334PROSITE-ProRule annotation
Disulfide bondi327 ↔ 350PROSITE-ProRule annotation
Disulfide bondi353 ↔ 362PROSITE-ProRule annotation
Disulfide bondi365 ↔ 378PROSITE-ProRule annotation
Disulfide bondi381 ↔ 393PROSITE-ProRule annotation
Disulfide bondi383 ↔ 399PROSITE-ProRule annotation
Disulfide bondi401 ↔ 410PROSITE-ProRule annotation
Disulfide bondi413 ↔ 425PROSITE-ProRule annotation
Disulfide bondi428 ↔ 439PROSITE-ProRule annotation
Disulfide bondi430 ↔ 446PROSITE-ProRule annotation
Disulfide bondi448 ↔ 457PROSITE-ProRule annotation
Disulfide bondi460 ↔ 475PROSITE-ProRule annotation
Glycosylationi559 – 5591N-linked (GlcNAc...)Sequence analysis
Glycosylationi633 – 6331N-linked (GlcNAc...)Sequence analysis
Disulfide bondi707 ↔ 716PROSITE-ProRule annotation
Disulfide bondi709 ↔ 723PROSITE-ProRule annotation
Disulfide bondi725 ↔ 734PROSITE-ProRule annotation
Disulfide bondi737 ↔ 753PROSITE-ProRule annotation
Disulfide bondi756 ↔ 764PROSITE-ProRule annotation
Disulfide bondi758 ↔ 775PROSITE-ProRule annotation
Disulfide bondi778 ↔ 787PROSITE-ProRule annotation
Disulfide bondi790 ↔ 808PROSITE-ProRule annotation
Disulfide bondi811 ↔ 825PROSITE-ProRule annotation
Disulfide bondi813 ↔ 832PROSITE-ProRule annotation
Disulfide bondi835 ↔ 844PROSITE-ProRule annotation
Disulfide bondi847 ↔ 864PROSITE-ProRule annotation
Disulfide bondi867 ↔ 881PROSITE-ProRule annotation
Disulfide bondi869 ↔ 888PROSITE-ProRule annotation
Disulfide bondi890 ↔ 899PROSITE-ProRule annotation
Disulfide bondi902 ↔ 915PROSITE-ProRule annotation
Disulfide bondi918 ↔ 930PROSITE-ProRule annotation
Disulfide bondi920 ↔ 937PROSITE-ProRule annotation
Disulfide bondi939 ↔ 948PROSITE-ProRule annotation
Disulfide bondi951 ↔ 963PROSITE-ProRule annotation
Disulfide bondi966 ↔ 978PROSITE-ProRule annotation
Disulfide bondi968 ↔ 984PROSITE-ProRule annotation
Disulfide bondi986 ↔ 995PROSITE-ProRule annotation
Disulfide bondi998 ↔ 1011PROSITE-ProRule annotation
Glycosylationi1005 – 10051N-linked (GlcNAc...)Sequence analysis
Glycosylationi1041 – 10411N-linked (GlcNAc...)Sequence analysis
Glycosylationi1048 – 10481N-linked (GlcNAc...)Sequence analysis
Glycosylationi1090 – 10901N-linked (GlcNAc...)Sequence analysis
Glycosylationi1144 – 11441N-linked (GlcNAc...)Sequence analysis
Glycosylationi1158 – 11581N-linked (GlcNAc...)Sequence analysis
Glycosylationi1188 – 11881N-linked (GlcNAc...)Sequence analysis
Glycosylationi1206 – 12061N-linked (GlcNAc...)Sequence analysis
Glycosylationi1253 – 12531N-linked (GlcNAc...)Sequence analysis
Glycosylationi1363 – 13631N-linked (GlcNAc...)Sequence analysis
Glycosylationi1386 – 13861N-linked (GlcNAc...)Sequence analysis
Glycosylationi1477 – 14771N-linked (GlcNAc...)Sequence analysis
Glycosylationi1487 – 14871N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiA0JP86.

Interactioni

Subunit structurei

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end.By similarity

Protein-protein interaction databases

STRINGi8364.ENSXETP00000027398.

Structurei

3D structure databases

ProteinModelPortaliA0JP86.
SMRiA0JP86. Positions 754-917.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 268240Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini269 – 32456Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini325 – 38056Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini381 – 42747Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini428 – 47750Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini504 – 672169Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini707 – 75549Laminin EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini756 – 81055Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini811 – 86656Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini867 – 91751Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini918 – 96548Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini966 – 101348Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1013 – 1592580Domain II and IBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1018 – 1477460Sequence analysisAdd
BLAST
Coiled coili1515 – 157965Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 10 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiA0JP86.
KOiK05635.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 11 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A0JP86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAPVLAVLA VLLLGTVRAA MDECYEEGSP QRCMPEFVNA AFNATVVATN
60 70 80 90 100
TCGTPPEEYC VQTGVTGVTK SCHICDSGQF HLQHGAEYLT DYNNQAEITW
110 120 130 140 150
WQSQTMLAGI QYPSTINLTL HLGKAFDITY VRLKFHTSRP ESFALYKRTH
160 170 180 190 200
EDGPWIPYQY YSGSCEKTYQ KFNRGFIRTG EDEQQALCTD EFSDISPLTG
210 220 230 240 250
GNVAFSTLEG RPSAYNFDNS PVLQEWVTAT DIRVTLNRLN TFGDEVFSDP
260 270 280 290 300
KVLKSYYYAI SDFAVGGRCK CNGHASECVR NEFEKIVCNC KHNTFGSDCE
310 320 330 340 350
KCLPFYNDRP WRRSTADSPN ECLPCNCNGR SQECYFDPEL YRSTGHGGHC
360 370 380 390 400
TGCADNTDGP NCERCRENYY RQDNNEPCHA CQCNPVGSLS TQCDNYGRCS
410 420 430 440 450
CKPGVMGEKC DRCQPGFHSL TEAGCRPCAC NPAGSTDECN VETGRCSCKD
460 470 480 490 500
NVEGFNCERC KPGFFHLDEA NPRGCTPCFC YGHSSVCSSA EGYRVSSIVS
510 520 530 540 550
TFESGVEGWT AQQRDGSEYS LSWVSDSSAV SVISESYFPI YFIAPAKFLG
560 570 580 590 600
NQGASYGQNL TFSFRVERRD TRLSAEDLVL EGAGLRVSVP LIAQGNSYPS
610 620 630 640 650
ETTQRYIFRM HEATDYPWRP SVSPFEFQKM LQNLTAIKIR GSYSERSAGF
660 670 680 690 700
LEEVSLVTAV AGAGPSAPWV EICSCPTGYI GQFCERCAPG YRRENPSQGP
710 720 730 740 750
YSPCVLCTCN GHSDTCDPES GVCDCQHNTA GPHCERCSEG YYGDSTTGSA
760 770 780 790 800
SDCQPCPCPG GSSCAVVPRT KEVVCTNCPL GTTGKRCELC DDGYFGDPLG
810 820 830 840 850
ENGAPRPCRI CECSNNIDPN AVGNCDRLTG ECLKCIYNTG GFYCDRCRDG
860 870 880 890 900
FYGNPLAQNP DLKCRACSCN PYGTVKGQSG CNQVTGQCEC LPHVTERDCS
910 920 930 940 950
ACEPGFYNLL SGRGCERCDC HSLGSTSGQC DVRTGQCECH PGISGQQCQQ
960 970 980 990 1000
CEPNHFGFGP EGCKPCDCDP EGSGSLQCKE DGRCECKSGF VGTRCDQCEE
1010 1020 1030 1040 1050
NYFYNRSGPG CQECPACYRL VKDKVNEQRG KLQELEDLLK NLSTGEENIT
1060 1070 1080 1090 1100
DQAFEERLRE AEKAVNDLLL DAQSSKDVDQ GMLDRLAEIN TTLSFQLERL
1110 1120 1130 1140 1150
QNIRDMIRDT DKQAQEARDR VENTEFIIDS ARVQLEKAKM AIANVSITPP
1160 1170 1180 1190 1200
ESTGDPNNMT LLAEEARKLA ERHMQEARDI EKAAKEANDT ANEALRLLQK
1210 1220 1230 1240 1250
TLASENQTAL DIEELNRKYA QAKDIARELE KQASKVHAEA EEAGNRALQI
1260 1270 1280 1290 1300
YANLTSVPSI DTTALQNEAD KIQKEAEELD SLIDRKLRDY EDLREDMRGR
1310 1320 1330 1340 1350
EMEVKNLLDK GKTEQQTADQ LLARADAAKA QAEEAAKKGR ETLQEANDIL
1360 1370 1380 1390 1400
NKLRDFDKRV NDNKTAAEAA LRKIPMIAQT IAEANNKTRQ AESALGNANA
1410 1420 1430 1440 1450
DARGAKSKAE EAEALANTVQ KKAATARAEA DNTFKEVTDL DGELQDMLQQ
1460 1470 1480 1490 1500
LQEAENQLKK KQAEAESDEK MAEMASNATK DAESNANNSK KSVNGVLATI
1510 1520 1530 1540 1550
DELLSRLGQL DSVDVGQLTV LEKTLDDAKN QLRDSDLDRK LAELQESSNL
1560 1570 1580 1590
QRVALDSYSR DIDQILRDIA NLEDIKNTLP AGCYNTPIIE KP
Length:1,592
Mass (Da):175,580
Last modified:December 12, 2006 - v1
Checksum:i458E53775436C3CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC127297 mRNA. Translation: AAI27298.1.
RefSeqiNP_001090659.1. NM_001097190.1.
UniGeneiStr.31506.

Genome annotation databases

GeneIDi100036631.
KEGGixtr:100036631.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC127297 mRNA. Translation: AAI27298.1.
RefSeqiNP_001090659.1. NM_001097190.1.
UniGeneiStr.31506.

3D structure databases

ProteinModelPortaliA0JP86.
SMRiA0JP86. Positions 754-917.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi8364.ENSXETP00000027398.

Proteomic databases

PaxDbiA0JP86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100036631.
KEGGixtr:100036631.

Organism-specific databases

CTDi3915.
XenbaseiXB-GENE-478553. lamc1.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiA0JP86.
KOiK05635.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 11 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.

Entry informationi

Entry nameiLAMC1_XENTR
AccessioniPrimary (citable) accession number: A0JP86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: December 12, 2006
Last modified: May 11, 2016
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.