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Protein

Laminin subunit gamma-2

Gene

LAMC2

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 4 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. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-2
Alternative name(s):
Epiligrin subunit gamma
Kalinin subunit gamma
Laminin-5 subunit gamma
Nicein subunit gamma
Gene namesi
Name:LAMC2
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Unplaced

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 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001707622 – 1190Laminin subunit gamma-2Add BLAST1169

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 37PROSITE-ProRule annotation
Disulfide bondi30 ↔ 53PROSITE-ProRule annotation
Disulfide bondi56 ↔ 65PROSITE-ProRule annotation
Disulfide bondi68 ↔ 81PROSITE-ProRule annotation
Disulfide bondi84 ↔ 96PROSITE-ProRule annotation
Disulfide bondi86 ↔ 102PROSITE-ProRule annotation
Disulfide bondi104 ↔ 113PROSITE-ProRule annotation
Disulfide bondi116 ↔ 128PROSITE-ProRule annotation
Disulfide bondi139 ↔ 150PROSITE-ProRule annotation
Disulfide bondi141 ↔ 155PROSITE-ProRule annotation
Disulfide bondi157 ↔ 166PROSITE-ProRule annotation
Disulfide bondi169 ↔ 184PROSITE-ProRule annotation
Glycosylationi342N-linked (GlcNAc...)Sequence analysis1
Glycosylationi362N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi463 ↔ 471PROSITE-ProRule annotation
Disulfide bondi465 ↔ 482PROSITE-ProRule annotation
Disulfide bondi485 ↔ 494PROSITE-ProRule annotation
Disulfide bondi497 ↔ 515PROSITE-ProRule annotation
Disulfide bondi518 ↔ 532PROSITE-ProRule annotation
Disulfide bondi520 ↔ 539PROSITE-ProRule annotation
Disulfide bondi542 ↔ 551PROSITE-ProRule annotation
Disulfide bondi554 ↔ 571PROSITE-ProRule annotation
Disulfide bondi574 ↔ 586PROSITE-ProRule annotation
Disulfide bondi576 ↔ 592PROSITE-ProRule annotation
Disulfide bondi594 ↔ 603PROSITE-ProRule annotation
Disulfide bondi611InterchainPROSITE-ProRule annotation
Disulfide bondi614InterchainPROSITE-ProRule annotation
Glycosylationi939N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1030N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1181InterchainPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8HZI9.
PRIDEiQ8HZI9.

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. Gamma-2 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).

Protein-protein interaction databases

STRINGi9796.ENSECAP00000019347.

Structurei

3D structure databases

ProteinModelPortaliQ8HZI9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 83Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST56
Domaini84 – 130Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST47
Domaini139 – 186Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST48
Domaini187 – 196Laminin EGF-like 4; first partPROSITE-ProRule annotation10
Domaini213 – 381Laminin IV type APROSITE-ProRule annotationAdd BLAST169
Domaini382 – 415Laminin EGF-like 4; second partPROSITE-ProRule annotationAdd BLAST34
Domaini416 – 462Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST47
Domaini463 – 517Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST55
Domaini518 – 573Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST56
Domaini574 – 603Laminin EGF-like 8; truncatedPROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni604 – 1190Domain II and IBy similarityAdd BLAST587

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili613 – 718Sequence analysisAdd BLAST106
Coiled coili809 – 1073Sequence analysisAdd BLAST265
Coiled coili1114 – 1190Sequence analysisAdd BLAST77

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain IV is globular.

Sequence similaritiesi

Contains 8 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IP6C. Eukaryota.
ENOG4110QI9. LUCA.
HOGENOMiHOG000019301.
HOVERGENiHBG062127.
InParanoidiQ8HZI9.
KOiK06246.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 7 hits.
[Graphical view]
SMARTiSM00181. EGF. 7 hits.
SM00180. EGF_Lam. 6 hits.
SM00281. LamB. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 6 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51115. LAMININ_IVA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8HZI9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPALWLRCGL CLALLLPAAR ASSGSQVCDC NGKSRQCIFD QELHKQTGNG
60 70 80 90 100
FRCLNCNDNT DGIHCERCKA GFYRQRERDR CLPCNCNSKG SLSARCDNSG
110 120 130 140 150
RCSCKPGVTG DRCDRCLPGF HTLTDAGCAQ DQRLLDSKCD CDPAGISGPC
160 170 180 190 200
DSGRCVCKPA VTGERCDRCR PGYYHLDGGN PQGCTQCFCY GHSASCHSSG
210 220 230 240 250
DYSVHKIISA FHQDVDGWKA VQRNGSPAKL QWSQRHRDIF SSARRSDPVY
260 270 280 290 300
FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL
310 320 330 340 350
MPLSKTLPCG ITKTYTFRLN EHPSSNWSPQ LSYFEYRRLL RNLTALRIRA
360 370 380 390 400
TYGEYSTGYI DNVTLISARP VSGAPAPWVE QCVCPVGYKG QFCQDCASGY
410 420 430 440 450
KRDSARLGPF GTCIPCNCQG GGACDPDTGD CYSGDENPDI PECADCPIGF
460 470 480 490 500
YNDPQDPRSC KPCPCRNGFS CSVMPETEEV VCNNCPQGVT GARCELCADG
510 520 530 540 550
YFGDPFGERG PVRPCQPCQC NNNVDPSASG NCDRLTGRCL KCIHNTAGVH
560 570 580 590 600
CDQCKAGYYG DPLAPNPADK CRACNCNPVG SEPVECRSDG SCVCKPGFGG
610 620 630 640 650
LSCEHAALTS CPACYNQVKV QMDQFMQQLQ ILEALISKAQ GGAVPNAELE
660 670 680 690 700
GRMQQAEQAL RDILREAQIS QDAVRSFNLR VAKARTQENS YRDRLDDLKM
710 720 730 740 750
TVERVRALGS QYQNQVQDTR RLITQMRLSL EESEASLQNT NIPPSEHYVG
760 770 780 790 800
PNGFKSLAQE ATRLADSHVQ SASNMEQLAK ETQEYSKELM SLVREALQEG
810 820 830 840 850
GGSGSLDGAV VQRLVGKLQK TKSLAQELSR EATQTDMEAD RSYQHSLHLL
860 870 880 890 900
NSVSQIQGVN DQSLQVEAKR LRQKADSLSN RVTKHMDEFK HVQSNLGNWE
910 920 930 940 950
EETRQLLQNG KNGRQTSDQL LSRANLAKSR AQEALSMGNA TFYEVENILK
960 970 980 990 1000
NLREFDLQVG DKRAEAEEAM KRLSYISQKV AGASDKTKQA EAALGSAAAD
1010 1020 1030 1040 1050
AQRAKNAARE ALEISGKIEQ EIGGLNLEAN VTADGALAME KGLATLKSEM
1060 1070 1080 1090 1100
REVEGELSRK EQEFDMDMDA VQMVIAEAQR VENRAKNAGV TIQDTLNTLD
1110 1120 1130 1140 1150
GILHLIDQPG SVDEERLILL EQKLFRAKTQ INSQLRPLMS ELEERAHRQK
1160 1170 1180 1190
GHLRFLETSI DGILADVKNL ENIRDNLPPG CYNTQALEQQ
Length:1,190
Mass (Da):130,846
Last modified:March 1, 2003 - v1
Checksum:i5F8C8BAC3E93A595
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY082802 mRNA. Translation: AAM03454.1.
RefSeqiNP_001075237.1. NM_001081768.1.
UniGeneiEca.12918.

Genome annotation databases

GeneIDi791245.
KEGGiecb:791245.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY082802 mRNA. Translation: AAM03454.1.
RefSeqiNP_001075237.1. NM_001081768.1.
UniGeneiEca.12918.

3D structure databases

ProteinModelPortaliQ8HZI9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000019347.

Proteomic databases

PaxDbiQ8HZI9.
PRIDEiQ8HZI9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi791245.
KEGGiecb:791245.

Organism-specific databases

CTDi3918.

Phylogenomic databases

eggNOGiENOG410IP6C. Eukaryota.
ENOG4110QI9. LUCA.
HOGENOMiHOG000019301.
HOVERGENiHBG062127.
InParanoidiQ8HZI9.
KOiK06246.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 7 hits.
[Graphical view]
SMARTiSM00181. EGF. 7 hits.
SM00180. EGF_Lam. 6 hits.
SM00281. LamB. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 6 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51115. LAMININ_IVA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMC2_HORSE
AccessioniPrimary (citable) accession number: Q8HZI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds heparin.By similarity

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.