| Tag | Content |
|---|
| CPLM ID | CPLM-012196 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Laminin subunit gamma-2 |
Protein Synonyms/Alias | Cell-scattering factor 140 kDa subunit; CSF 140 kDa subunit; Epiligrin subunit gamma; Kalinin subunit gamma; Kalinin/nicein/epiligrin 100 kDa subunit; Ladsin 140 kDa subunit; Laminin B2t chain; Laminin-5 subunit gamma; Large adhesive scatter factor 140 kDa subunit; Nicein subunit gamma |
Gene Name | LAMC2 |
Gene Synonyms/Alias | LAMB2T; LAMNB2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 636 | RMEALISKAQGGDGV | ubiquitination | [1] |
|
Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 28 83 Laminin EGF-like 1.
DOMAIN 84 130 Laminin EGF-like 2.
DOMAIN 139 186 Laminin EGF-like 3.
DOMAIN 187 196 Laminin EGF-like 4; first part.
DOMAIN 213 381 Laminin IV type A.
DOMAIN 382 415 Laminin EGF-like 4; second part.
DOMAIN 416 461 Laminin EGF-like 5.
DOMAIN 462 516 Laminin EGF-like 6.
DOMAIN 517 572 Laminin EGF-like 7.
DOMAIN 573 602 Laminin EGF-like 8; truncated.
REGION 603 1193 Domain II and I.
CARBOHYD 342 342 N-linked (GlcNAc...) (Potential).
CARBOHYD 362 362 N-linked (GlcNAc...) (Potential).
CARBOHYD 942 942 N-linked (GlcNAc...) (Potential).
CARBOHYD 1033 1033 N-linked (GlcNAc...) (Potential).
DISULFID 28 37 By similarity.
DISULFID 30 53 By similarity.
DISULFID 56 65 By similarity.
DISULFID 68 81 By similarity.
DISULFID 84 96 By similarity.
DISULFID 86 102 By similarity.
DISULFID 104 113 By similarity.
DISULFID 116 128 By similarity.
DISULFID 139 150 By similarity.
DISULFID 141 155 By similarity.
DISULFID 157 166 By similarity.
DISULFID 169 184 By similarity.
DISULFID 462 470 By similarity.
DISULFID 464 481 By similarity.
DISULFID 484 493 By similarity.
DISULFID 496 514 By similarity.
DISULFID 517 531 By similarity.
DISULFID 519 538 By similarity.
DISULFID 541 550 By similarity.
DISULFID 553 570 By similarity.
DISULFID 573 585 By similarity.
DISULFID 575 591 By similarity.
DISULFID 593 602 By similarity.
DISULFID 609 609 Interchain (Probable).
DISULFID 612 612 Interchain (Probable).
DISULFID 1184 1184 Interchain (Probable). |
Keyword | Alternative splicing; Basement membrane; Cell adhesion; Coiled coil; Complete proteome; Direct protein sequencing; Disulfide bond; Epidermolysis bullosa; Extracellular matrix; Glycoprotein; Heparin-binding; Laminin EGF-like domain; Polymorphism; Reference proteome; Repeat; Secreted; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1193 AA |
Protein Sequence | MPALWLGCCL CFSLLLPAAR ATSRREVCDC NGKSRQCIFD RELHRQTGNG FRCLNCNDNT 60
DGIHCEKCKN GFYRHRERDR CLPCNCNSKG SLSARCDNSG RCSCKPGVTG ARCDRCLPGF 120
HMLTDAGCTQ DQRLLDSKCD CDPAGIAGPC DAGRCVCKPA VTGERCDRCR SGYYNLDGGN 180
PEGCTQCFCY GHSASCRSSA EYSVHKITST FHQDVDGWKA VQRNGSPAKL QWSQRHQDVF 240
SSAQRLDPVY FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL 300
MPLGKTLPCG LTKTYTFRLN EHPSNNWSPQ LSYFEYRRLL RNLTALRIRA TYGEYSTGYI 360
DNVTLISARP VSGAPAPWVE QCICPVGYKG QFCQDCASGY KRDSARLGPF GTCIPCNCQG 420
GGACDPDTGD CYSGDENPDI ECADCPIGFY NDPHDPRSCK PCPCHNGFSC SVMPETEEVV 480
CNNCPPGVTG ARCELCADGY FGDPFGEHGP VRPCQPCQCN NNVDPSASGN CDRLTGRCLK 540
CIHNTAGIYC DQCKAGYFGD PLAPNPADKC RACNCNPMGS EPVGCRSDGT CVCKPGFGGP 600
NCEHGAFSCP ACYNQVKIQM DQFMQQLQRM EALISKAQGG DGVVPDTELE GRMQQAEQAL 660
QDILRDAQIS EGASRSLGLQ LAKVRSQENS YQSRLDDLKM TVERVRALGS QYQNRVRDTH 720
RLITQMQLSL AESEASLGNT NIPASDHYVG PNGFKSLAQE ATRLAESHVE SASNMEQLTR 780
ETEDYSKQAL SLVRKALHEG VGSGSGSPDG AVVQGLVEKL EKTKSLAQQL TREATQAEIE 840
ADRSYQHSLR LLDSVSRLQG VSDQSFQVEE AKRIKQKADS LSSLVTRHMD EFKRTQKNLG 900
NWKEEAQQLL QNGKSGREKS DQLLSRANLA KSRAQEALSM GNATFYEVES ILKNLREFDL 960
QVDNRKAEAE EAMKRLSYIS QKVSDASDKT QQAERALGSA AADAQRAKNG AGEALEISSE 1020
IEQEIGSLNL EANVTADGAL AMEKGLASLK SEMREVEGEL ERKELEFDTN MDAVQMVITE 1080
AQKVDTRAKN AGVTIQDTLN TLDGLLHLMD QPLSVDEEGL VLLEQKLSRA KTQINSQLRP 1140
MMSELEERAR QQRGHLHLLE TSIDGILADV KNLENIRDNL PPGCYNTQAL EQQ 1193 |
Gene Ontology | GO:0005576; C:extracellular region; TAS:Reactome. GO:0005610; C:laminin-5 complex; IEA:Compara. GO:0008201; F:heparin binding; IEA:UniProtKB-KW. GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. GO:0008544; P:epidermis development; TAS:ProtInc. GO:0030198; P:extracellular matrix organization; TAS:Reactome. GO:0031581; P:hemidesmosome assembly; TAS:Reactome. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |