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Protein

Laminin subunit gamma-1

Gene

lamc1

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 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

  • axon guidance Source: ZFIN
  • brain development Source: ZFIN
  • brain morphogenesis Source: ZFIN
  • cell adhesion Source: UniProtKB-KW
  • detection of light stimulus involved in visual perception Source: ZFIN
  • eye development Source: ZFIN
  • muscle organ development Source: ZFIN
  • notochord development Source: ZFIN
  • notochord morphogenesis Source: ZFIN
  • optokinetic behavior Source: ZFIN
  • retinal ganglion cell axon guidance Source: ZFIN
  • skeletal muscle tissue development Source: ZFIN
  • somite development Source: ZFIN
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-DRE-3000157. Laminin interactions.
R-DRE-8874081. MET activates PTK2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-1
Gene namesi
Name:lamc1
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 2

Organism-specific databases

ZFINiZDB-GENE-021226-3. lamc1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000036420120 – 1593Laminin subunit gamma-1Add BLAST1574

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi44N-linked (GlcNAc...)Sequence analysis1
Glycosylationi118N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi270 ↔ 279PROSITE-ProRule annotation
Disulfide bondi272 ↔ 289PROSITE-ProRule annotation
Disulfide bondi291 ↔ 300PROSITE-ProRule annotation
Disulfide bondi303 ↔ 323PROSITE-ProRule annotation
Disulfide bondi326 ↔ 335PROSITE-ProRule annotation
Disulfide bondi328 ↔ 351PROSITE-ProRule annotation
Disulfide bondi354 ↔ 363PROSITE-ProRule annotation
Disulfide bondi366 ↔ 379PROSITE-ProRule annotation
Disulfide bondi382 ↔ 394PROSITE-ProRule annotation
Disulfide bondi384 ↔ 400PROSITE-ProRule annotation
Disulfide bondi402 ↔ 411PROSITE-ProRule annotation
Disulfide bondi414 ↔ 426PROSITE-ProRule annotation
Disulfide bondi429 ↔ 440PROSITE-ProRule annotation
Disulfide bondi431 ↔ 447PROSITE-ProRule annotation
Disulfide bondi449 ↔ 458PROSITE-ProRule annotation
Disulfide bondi461 ↔ 476PROSITE-ProRule annotation
Glycosylationi560N-linked (GlcNAc...)Sequence analysis1
Glycosylationi634N-linked (GlcNAc...)Sequence analysis1
Glycosylationi654N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi708 ↔ 717PROSITE-ProRule annotation
Disulfide bondi710 ↔ 724PROSITE-ProRule annotation
Disulfide bondi726 ↔ 735PROSITE-ProRule annotation
Disulfide bondi738 ↔ 754PROSITE-ProRule annotation
Disulfide bondi757 ↔ 765PROSITE-ProRule annotation
Disulfide bondi759 ↔ 776PROSITE-ProRule annotation
Disulfide bondi779 ↔ 788PROSITE-ProRule annotation
Disulfide bondi791 ↔ 809PROSITE-ProRule annotation
Disulfide bondi812 ↔ 826PROSITE-ProRule annotation
Disulfide bondi814 ↔ 833PROSITE-ProRule annotation
Disulfide bondi836 ↔ 845PROSITE-ProRule annotation
Disulfide bondi848 ↔ 865PROSITE-ProRule annotation
Disulfide bondi868 ↔ 882PROSITE-ProRule annotation
Disulfide bondi870 ↔ 889PROSITE-ProRule annotation
Disulfide bondi891 ↔ 900PROSITE-ProRule annotation
Disulfide bondi903 ↔ 916PROSITE-ProRule annotation
Disulfide bondi919 ↔ 931PROSITE-ProRule annotation
Disulfide bondi921 ↔ 938PROSITE-ProRule annotation
Disulfide bondi940 ↔ 949PROSITE-ProRule annotation
Disulfide bondi952 ↔ 964PROSITE-ProRule annotation
Disulfide bondi967 ↔ 979PROSITE-ProRule annotation
Disulfide bondi969 ↔ 985PROSITE-ProRule annotation
Disulfide bondi987 ↔ 996PROSITE-ProRule annotation
Disulfide bondi999 ↔ 1012PROSITE-ProRule annotation
Glycosylationi1006N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1091N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1159N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1189N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1207N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1254N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1364N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1379N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ1LVF0.
PeptideAtlasiQ1LVF0.
PRIDEiQ1LVF0.

Expressioni

Gene expression databases

BgeeiENSDARG00000036279.

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

STRINGi7955.ENSDARP00000024860.

Structurei

3D structure databases

ProteinModelPortaliQ1LVF0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 269Laminin N-terminalPROSITE-ProRule annotationAdd BLAST240
Domaini270 – 325Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST56
Domaini326 – 381Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST56
Domaini382 – 428Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Domaini429 – 478Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST50
Domaini505 – 673Laminin IV type APROSITE-ProRule annotationAdd BLAST169
Domaini708 – 756Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST49
Domaini757 – 811Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST55
Domaini812 – 867Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST56
Domaini868 – 918Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST51
Domaini919 – 966Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST48
Domaini967 – 1014Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST48

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1014 – 1593Domain II and IBy similarityAdd BLAST580

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1021 – 1580Sequence analysisAdd BLAST560

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.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiQ1LVF0.
KOiK05635.
OMAiLCACNGH.
OrthoDBiEOG091G005L.
PhylomeDBiQ1LVF0.
TreeFamiTF352481.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 5 hits.
SM00180. EGF_Lam. 10 hits.
SM01411. Ephrin_rec_like. 4 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.

Q1LVF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLFSCLLLW TLWAACSHGA MDECIDEDDR PQRCMPEFVN AAFNATVVAT
60 70 80 90 100
NTCGSPPEEF CVQTGVTGVT KSCHICNAAD PRLHHGAVYL TDYNQPVQPT
110 120 130 140 150
WWQSQTMLAG IQYPNSINLT LHLGKSFDIT YVRLKFHTSR PESFAIYKRS
160 170 180 190 200
SEDGPWTPYQ YYSGSCEKTY SKNNRGFIRT GEDEQQALCT DEFSDISPLY
210 220 230 240 250
GGNVAFSTLE GRPSAYNFDN SPVLQDWVTA TDIRVTLNRL NTFGDEVFND
260 270 280 290 300
PKVLKSYYYA ISDFAVGGRC KCNGHASECV KNEYSKLVCN CKHNTEGADC
310 320 330 340 350
NVCKPFYNDR PWRRATAENP NECLPCNCNG KSAECYFDPE LYRATGHGGH
360 370 380 390 400
CRNCADNTDG PKCERCLANY YREASGQRCL SCGCNPVGSL STQCDNTGRC
410 420 430 440 450
SCKPGVMGDK CDRCQPGYHS LSEAGCRPCS CNPAGSTQEC DVQTGRCQCK
460 470 480 490 500
ENVDGFNCDR CKLGYFNLDP QNPQGCTPCF CFQHSTVCES ADGYSVHKIT
510 520 530 540 550
STFDRDDEGW KGKQRDDSSV PVQWSPSSGE ISLISEDYFP IYFVAPDKFL
560 570 580 590 600
HNQLLSYGQN LTLNFRIQRH DARLSAEDVV LEGSGLRVAV PLIAQGNSYP
610 620 630 640 650
GEETQTFVFR LHDTTDYPWR PTIKHADFQK LLYNLTSIMI RGTYSAQSAG
660 670 680 690 700
YLDNVSLVTA RRGPGTPARW VEKCTCPQGY LGQHCEQCDQ GFRRSRPELR
710 720 730 740 750
RFSTCERCNC NGHSDTCDPE TGMCNCQHNT AGLSCERCKD GFYGDSTVGS
760 770 780 790 800
SSDCKACPCP AGATCAVVPK TNEVVCTNCP TGTTGKRCEL CDDGFFGDPL
810 820 830 840 850
GEKGPVRACR ACSCNNNIDP NAVGNCNRES GECLKCIYNT AGVFCDRCKQ
860 870 880 890 900
GFYGDARAAN VADKCKPCKC SPYGTVDRQT ACSQVTGQCP CLPHVINRDC
910 920 930 940 950
GACELGFYNL QSGKGCERCN CNPIGSTNGQ CDIVSGQCEC QPGVTGQHCE
960 970 980 990 1000
RCEVNFFGFS SSGCKPCDCD PEGSESAQCK EDGRCHCRPG FVGSRCDMCE
1010 1020 1030 1040 1050
ENYFYNRSTP GCQQCPNCYS LVRDKVNQQR QKLLDLQNLI DSLDNTETTV
1060 1070 1080 1090 1100
SDKAFEDRLK EAEKTIMDLL EEAQASKEVD KGLLDRLNNI NKTLNNQWNR
1110 1120 1130 1140 1150
LQNIKNTVDN TGAQADRARN RVRDAENLIN TAREELDKAK EAISKVDIKI
1160 1170 1180 1190 1200
PTTSGDPNNM TLLAEEARKL SEKHKADADQ IEKIAKDAND TSTKAYNMLK
1210 1220 1230 1240 1250
KALDGENKTS SDIDELNRKY LEAKDLAKNL EKQAAKVHAE AEEAGNKALK
1260 1270 1280 1290 1300
IYANLTSLPP INTKTLEDDA NKIKKEASDL DKLIDKTEKE YNDLREDLRG
1310 1320 1330 1340 1350
KETEVRKLLD KGKTEQQTAD QLLARADAAK ALAEEAAKKG KSTFQEAQDI
1360 1370 1380 1390 1400
LNNLRDFDKR VNDNKTAAED AMRRIPQINA TINEANDKTR RAEAALGNAA
1410 1420 1430 1440 1450
ADAKDAKAKA EEAEKIANDV QKGSAKTKAD AEKAFEDTMK LDKDVDKMMD
1460 1470 1480 1490 1500
QLTAAEKELE KKKAEADTDM MMASMASDNA KDAEGNARKA KSAVREVLNT
1510 1520 1530 1540 1550
INALLGQLGN IDKVDLSKLN QIDNALKDAK DKMAGSELDR KLKELNDIAK
1560 1570 1580 1590
SQEDMISDYD RQIQEIRADI ANLNDIKNTL PEGCFNTPSL ERP
Length:1,593
Mass (Da):176,206
Last modified:February 20, 2007 - v2
Checksum:i3A7982905896D403
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti819D → E in AAM61766 (PubMed:12070089).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF468048 mRNA. Translation: AAM61766.1.
BX681417, BX571812 Genomic DNA. Translation: CAK05288.2.
BX571812, BX681417 Genomic DNA. Translation: CAQ13276.1.
RefSeqiNP_775384.1. NM_173277.1.
UniGeneiDr.132970.

Genome annotation databases

EnsembliENSDART00000004277; ENSDARP00000024860; ENSDARG00000036279.
GeneIDi286832.
KEGGidre:286832.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF468048 mRNA. Translation: AAM61766.1.
BX681417, BX571812 Genomic DNA. Translation: CAK05288.2.
BX571812, BX681417 Genomic DNA. Translation: CAQ13276.1.
RefSeqiNP_775384.1. NM_173277.1.
UniGeneiDr.132970.

3D structure databases

ProteinModelPortaliQ1LVF0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000024860.

Proteomic databases

PaxDbiQ1LVF0.
PeptideAtlasiQ1LVF0.
PRIDEiQ1LVF0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000004277; ENSDARP00000024860; ENSDARG00000036279.
GeneIDi286832.
KEGGidre:286832.

Organism-specific databases

CTDi3915.
ZFINiZDB-GENE-021226-3. lamc1.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiQ1LVF0.
KOiK05635.
OMAiLCACNGH.
OrthoDBiEOG091G005L.
PhylomeDBiQ1LVF0.
TreeFamiTF352481.

Enzyme and pathway databases

ReactomeiR-DRE-3000157. Laminin interactions.
R-DRE-8874081. MET activates PTK2 signaling.

Miscellaneous databases

PROiQ1LVF0.

Gene expression databases

BgeeiENSDARG00000036279.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 5 hits.
SM00180. EGF_Lam. 10 hits.
SM01411. Ephrin_rec_like. 4 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...

Entry informationi

Entry nameiLAMC1_DANRE
AccessioniPrimary (citable) accession number: Q1LVF0
Secondary accession number(s): Q8JHV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: February 20, 2007
Last modified: November 30, 2016
This is version 86 of the entry and version 2 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.