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O15230 (LAMA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit alpha-5
Alternative name(s):
Laminin-10 subunit alpha
Laminin-11 subunit alpha
Laminin-15 subunit alpha
Gene names
Name:LAMA5
Synonyms:KIAA0533, KIAA1907
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3695 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Alpha-5 is a subunit of laminin-10 (laminin-511), laminin-11 (laminin-521) and laminin-15 (laminin-523).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Tissue specificity

Expressed in heart, lung, kidney, skeletal muscle, pancreas, retina and placenta. Little or no expression in brain and liver.

Domain

Domain G is globular and is part of the major cell-binding site located in the long arm of the laminin heterotrimer.

Sequence similarities

Contains 22 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Contains 1 laminin IV type A domain.

Contains 1 laminin N-terminal domain.

Sequence caution

The sequence CAC22310.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Laminin EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Non-traceable author statement Ref.1. Source: UniProtKB

branching involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Non-traceable author statement Ref.1. Source: UniProtKB

cell migration

Inferred from direct assay Ref.1. Source: UniProtKB

cell proliferation

Non-traceable author statement Ref.1. Source: UniProtKB

cell recognition

Non-traceable author statement Ref.1. Source: UniProtKB

cilium assembly

Inferred from electronic annotation. Source: Ensembl

cytoskeleton organization

Non-traceable author statement Ref.1. Source: UniProtKB

embryo development

Non-traceable author statement Ref.1. Source: UniProtKB

endothelial cell differentiation

Non-traceable author statement Ref.1. Source: UniProtKB

establishment of protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

focal adhesion assembly

Non-traceable author statement Ref.1. Source: UniProtKB

hair follicle development

Inferred from electronic annotation. Source: Ensembl

integrin-mediated signaling pathway

Inferred from mutant phenotype Ref.1. Source: UniProtKB

lung development

Inferred from electronic annotation. Source: Ensembl

morphogenesis of a polarized epithelium

Inferred from electronic annotation. Source: Ensembl

morphogenesis of embryonic epithelium

Inferred from electronic annotation. Source: Ensembl

muscle organ development

Inferred from electronic annotation. Source: Ensembl

neural crest cell migration

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion

Inferred from electronic annotation. Source: InterPro

regulation of cell migration

Inferred from electronic annotation. Source: InterPro

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of embryonic development

Inferred from electronic annotation. Source: InterPro

substrate adhesion-dependent cell spreading

Inferred from direct assay PubMed 16236823. Source: BHF-UCL

   Cellular_componentbasal lamina

Non-traceable author statement Ref.1. Source: UniProtKB

basement membrane

Inferred from direct assay PubMed 14557481. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 10964500. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

laminin-1 complex

Inferred from electronic annotation. Source: InterPro

laminin-10 complex

Inferred from direct assay PubMed 10964500. Source: UniProtKB

laminin-11 complex

Traceable author statement PubMed 16236823. Source: BHF-UCL

laminin-5 complex

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionintegrin binding

Inferred from direct assay Ref.1. Source: UniProtKB

structural molecule activity

Inferred by curator Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 36953660Laminin subunit alpha-5
PRO_0000017062

Regions

Domain41 – 299259Laminin N-terminal
Domain300 – 35859Laminin EGF-like 1
Domain359 – 42870Laminin EGF-like 2
Domain429 – 47446Laminin EGF-like 3
Domain494 – 54047Laminin EGF-like 4
Domain541 – 58646Laminin EGF-like 5
Domain587 – 63145Laminin EGF-like 6
Domain632 – 67645Laminin EGF-like 7
Domain677 – 72246Laminin EGF-like 8
Domain723 – 77553Laminin EGF-like 9
Domain776 – 82853Laminin EGF-like 10
Domain829 – 85022Laminin EGF-like 11; truncated
Domain1438 – 148346Laminin EGF-like 12
Domain1484 – 152744Laminin EGF-like 13
Domain1528 – 157649Laminin EGF-like 14
Domain1577 – 162751Laminin EGF-like 15
Domain1628 – 163710Laminin EGF-like 16; first part
Domain1641 – 1830190Laminin IV type A
Domain1831 – 186333Laminin EGF-like 16; second part
Domain1864 – 191249Laminin EGF-like 17
Domain1913 – 196856Laminin EGF-like 18
Domain1969 – 202254Laminin EGF-like 19
Domain2023 – 206947Laminin EGF-like 20
Domain2070 – 211647Laminin EGF-like 21
Domain2117 – 216650Laminin EGF-like 22
Domain2736 – 2929194Laminin G-like 1
Domain2941 – 3115175Laminin G-like 2
Domain3124 – 3292169Laminin G-like 3
Domain3340 – 3513174Laminin G-like 4
Domain3520 – 3692173Laminin G-like 5
Region851 – 1437587Domain IV 1 (domain IV B)
Region2167 – 2735569Domain II and I
Coiled coil2203 – 222119 Potential
Coiled coil2335 – 2466132 Potential
Coiled coil2510 – 2670161 Potential
Motif1722 – 17243Cell attachment site Potential
Motif1838 – 18403Cell attachment site Potential

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1431N-linked (GlcNAc...) Potential
Glycosylation2431N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Glycosylation4791N-linked (GlcNAc...) Potential
Glycosylation9001N-linked (GlcNAc...) Potential
Glycosylation9211N-linked (GlcNAc...) Potential
Glycosylation9591N-linked (GlcNAc...) Potential
Glycosylation13301N-linked (GlcNAc...) Potential
Glycosylation15291N-linked (GlcNAc...) Potential
Glycosylation15551N-linked (GlcNAc...) Potential
Glycosylation21961N-linked (GlcNAc...) Potential
Glycosylation22091N-linked (GlcNAc...) Ref.7
Glycosylation23031N-linked (GlcNAc...) Ref.7
Glycosylation24231N-linked (GlcNAc...) Ref.7
Glycosylation25011N-linked (GlcNAc...) Ref.7
Glycosylation25681N-linked (GlcNAc...) Ref.7
Glycosylation27071N-linked (GlcNAc...) Ref.7
Glycosylation31071N-linked (GlcNAc...) Ref.7
Glycosylation32091N-linked (GlcNAc...) Potential
Glycosylation32571N-linked (GlcNAc...) Potential
Glycosylation32871N-linked (GlcNAc...) Potential
Glycosylation36261N-linked (GlcNAc...) Potential
Disulfide bond300 ↔ 309 By similarity
Disulfide bond302 ↔ 322 By similarity
Disulfide bond324 ↔ 333 By similarity
Disulfide bond336 ↔ 356 By similarity
Disulfide bond359 ↔ 368 By similarity
Disulfide bond361 ↔ 393 By similarity
Disulfide bond396 ↔ 405 By similarity
Disulfide bond408 ↔ 426 By similarity
Disulfide bond429 ↔ 440 By similarity
Disulfide bond431 ↔ 447 By similarity
Disulfide bond449 ↔ 458 By similarity
Disulfide bond461 ↔ 471 By similarity
Disulfide bond494 ↔ 506 By similarity
Disulfide bond496 ↔ 515 By similarity
Disulfide bond517 ↔ 526 By similarity
Disulfide bond529 ↔ 538 By similarity
Disulfide bond541 ↔ 553 By similarity
Disulfide bond543 ↔ 560 By similarity
Disulfide bond562 ↔ 571 By similarity
Disulfide bond574 ↔ 584 By similarity
Disulfide bond587 ↔ 599 By similarity
Disulfide bond589 ↔ 605 By similarity
Disulfide bond607 ↔ 616 By similarity
Disulfide bond619 ↔ 629 By similarity
Disulfide bond632 ↔ 644 By similarity
Disulfide bond634 ↔ 650 By similarity
Disulfide bond652 ↔ 661 By similarity
Disulfide bond664 ↔ 674 By similarity
Disulfide bond677 ↔ 689 By similarity
Disulfide bond679 ↔ 696 By similarity
Disulfide bond698 ↔ 707 By similarity
Disulfide bond710 ↔ 725 By similarity
Disulfide bond746 ↔ 755 By similarity
Disulfide bond758 ↔ 773 By similarity
Disulfide bond776 ↔ 790 By similarity
Disulfide bond778 ↔ 797 By similarity
Disulfide bond799 ↔ 808 By similarity
Disulfide bond811 ↔ 826 By similarity
Disulfide bond829 ↔ 841 By similarity
Disulfide bond831 ↔ 848 By similarity
Disulfide bond850 ↔ 859 By similarity
Disulfide bond1438 ↔ 1450 By similarity
Disulfide bond1440 ↔ 1457 By similarity
Disulfide bond1459 ↔ 1468 By similarity
Disulfide bond1471 ↔ 1481 By similarity
Disulfide bond1484 ↔ 1491 By similarity
Disulfide bond1486 ↔ 1498 By similarity
Disulfide bond1500 ↔ 1509 By similarity
Disulfide bond1512 ↔ 1525 By similarity
Disulfide bond1528 ↔ 1543 By similarity
Disulfide bond1530 ↔ 1550 By similarity
Disulfide bond1552 ↔ 1561 By similarity
Disulfide bond1564 ↔ 1574 By similarity
Disulfide bond1577 ↔ 1589 By similarity
Disulfide bond1579 ↔ 1596 By similarity
Disulfide bond1598 ↔ 1607 By similarity
Disulfide bond1610 ↔ 1625 By similarity
Disulfide bond1864 ↔ 1873 By similarity
Disulfide bond1866 ↔ 1880 By similarity
Disulfide bond1883 ↔ 1892 By similarity
Disulfide bond1895 ↔ 1910 By similarity
Disulfide bond1913 ↔ 1928 By similarity
Disulfide bond1915 ↔ 1937 By similarity
Disulfide bond1939 ↔ 1948 By similarity
Disulfide bond1951 ↔ 1966 By similarity
Disulfide bond1969 ↔ 1984 By similarity
Disulfide bond1971 ↔ 1991 By similarity
Disulfide bond1994 ↔ 2003 By similarity
Disulfide bond2006 ↔ 2020 By similarity
Disulfide bond2023 ↔ 2033 By similarity
Disulfide bond2025 ↔ 2040 By similarity
Disulfide bond2042 ↔ 2051 By similarity
Disulfide bond2054 ↔ 2067 By similarity
Disulfide bond2070 ↔ 2081 By similarity
Disulfide bond2072 ↔ 2088 By similarity
Disulfide bond2090 ↔ 2099 By similarity
Disulfide bond2102 ↔ 2114 By similarity
Disulfide bond2117 ↔ 2124 By similarity
Disulfide bond2119 ↔ 2131 By similarity
Disulfide bond2133 ↔ 2142 By similarity
Disulfide bond2145 ↔ 2164 By similarity
Disulfide bond2167Interchain Probable
Disulfide bond2170Interchain Probable
Disulfide bond2899 ↔ 2929 By similarity
Disulfide bond3090 ↔ 3115 By similarity
Disulfide bond3261 ↔ 3292 By similarity
Disulfide bond3490 ↔ 3513 By similarity
Disulfide bond3664 ↔ 3692 By similarity

Natural variations

Natural variant4011T → A. Ref.1
Corresponds to variant rs4925229 [ dbSNP | Ensembl ].
VAR_047887
Natural variant8891V → M. Ref.3
Corresponds to variant rs6062223 [ dbSNP | Ensembl ].
VAR_030847
Natural variant12581M → T. Ref.1
Corresponds to variant rs3810548 [ dbSNP | Ensembl ].
VAR_030848
Natural variant13671K → E. Ref.1 Ref.3
Corresponds to variant rs2427286 [ dbSNP | Ensembl ].
VAR_030849
Natural variant14341G → A.
Corresponds to variant rs17750870 [ dbSNP | Ensembl ].
VAR_030850
Natural variant16671R → W.
Corresponds to variant rs13039398 [ dbSNP | Ensembl ].
VAR_030851
Natural variant16711T → M.
Corresponds to variant rs944893 [ dbSNP | Ensembl ].
VAR_047888
Natural variant17171H → Y.
Corresponds to variant rs875379 [ dbSNP | Ensembl ].
VAR_030852
Natural variant18071F → S. Ref.1 Ref.3
Corresponds to variant rs2427284 [ dbSNP | Ensembl ].
VAR_030853
Natural variant19001V → M. Ref.1
Corresponds to variant rs2427283 [ dbSNP | Ensembl ].
VAR_030854
Natural variant19081A → T.
Corresponds to variant rs11698080 [ dbSNP | Ensembl ].
VAR_030855
Natural variant20361H → R.
Corresponds to variant rs6143021 [ dbSNP | Ensembl ].
VAR_030856
Natural variant20531R → H.
Corresponds to variant rs3737137 [ dbSNP | Ensembl ].
VAR_030857
Natural variant20621D → N. Ref.1 Ref.4
Corresponds to variant rs2274934 [ dbSNP | Ensembl ].
VAR_030858
Natural variant22261R → H.
Corresponds to variant rs2297587 [ dbSNP | Ensembl ].
VAR_030859
Natural variant30791R → W. Ref.1 Ref.4 Ref.5
Corresponds to variant rs944895 [ dbSNP | Ensembl ].
VAR_030860

Experimental info

Sequence conflict9561T → A in AAM12527. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O15230 [UniParc].

Last modified January 11, 2011. Version 8.
Checksum: B13C479B55282E3C

FASTA3,695399,737
        10         20         30         40         50         60 
MAKRLCAGSA LCVRGPRGPA PLLLVGLALL GAARAREEAG GGFSLHPPYF NLAEGARIAA 

        70         80         90        100        110        120 
SATCGEEAPA RGSPRPTEDL YCKLVGGPVA GGDPNQTIRG QYCDICTAAN SNKAHPASNA 

       130        140        150        160        170        180 
IDGTERWWQS PPLSRGLEYN EVNVTLDLGQ VFHVAYVLIK FANSPRPDLW VLERSMDFGR 

       190        200        210        220        230        240 
TYQPWQFFAS SKRDCLERFG PQTLERITRD DAAICTTEYS RIVPLENGEI VVSLVNGRPG 

       250        260        270        280        290        300 
AMNFSYSPLL REFTKATNVR LRFLRTNTLL GHLMGKALRD PTVTRRYYYS IKDISIGGRC 

       310        320        330        340        350        360 
VCHGHADACD AKDPTDPFRL QCTCQHNTCG GTCDRCCPGF NQQPWKPATA NSANECQSCN 

       370        380        390        400        410        420 
CYGHATDCYY DPEVDRRRAS QSLDGTYQGG GVCIDCQHHT TGVNCERCLP GFYRSPNHPL 

       430        440        450        460        470        480 
DSPHVCRRCN CESDFTDGTC EDLTGRCYCR PNFSGERCDV CAEGFTGFPS CYPTPSSSND 

       490        500        510        520        530        540 
TREQVLPAGQ IVNCDCSAAG TQGNACRKDP RVGRCLCKPN FQGTHCELCA PGFYGPGCQP 

       550        560        570        580        590        600 
CQCSSPGVAD DRCDPDTGQC RCRVGFEGAT CDRCAPGYFH FPLCQLCGCS PAGTLPEGCD 

       610        620        630        640        650        660 
EAGRCLCQPE FAGPHCDRCR PGYHGFPNCQ ACTCDPRGAL DQLCGAGGLC RCRPGYTGTA 

       670        680        690        700        710        720 
CQECSPGFHG FPSCVPCHCS AEGSLHAACD PRSGQCSCRP RVTGLRCDTC VPGAYNFPYC 

       730        740        750        760        770        780 
EAGSCHPAGL APVDPALPEA QVPCMCRAHV EGPSCDRCKP GFWGLSPSNP EGCTRCSCDL 

       790        800        810        820        830        840 
RGTLGGVAEC QPGTGQCFCK PHVCGQACAS CKDGFFGLDQ ADYFGCRSCR CDIGGALGQS 

       850        860        870        880        890        900 
CEPRTGVCRC RPNTQGPTCS EPARDHYLPD LHHLRLELEE AATPEGHAVR FGFNPLEFEN 

       910        920        930        940        950        960 
FSWRGYAQMA PVQPRIVARL NLTSPDLFWL VFRYVNRGAM SVSGRVSVRE EGRSATCANC 

       970        980        990       1000       1010       1020 
TAQSQPVAFP PSTEPAFITV PQRGFGEPFV LNPGTWALRV EAEGVLLDYV VLLPSAYYEA 

      1030       1040       1050       1060       1070       1080 
ALLQLRVTEA CTYRPSAQQS GDNCLLYTHL PLDGFPSAAG LEALCRQDNS LPRPCPTEQL 

      1090       1100       1110       1120       1130       1140 
SPSHPPLITC TGSDVDVQLQ VAVPQPGRYA LVVEYANEDA RQEVGVAVHT PQRAPQQGLL 

      1150       1160       1170       1180       1190       1200 
SLHPCLYSTL CRGTARDTQD HLAVFHLDSE ASVRLTAEQA RFFLHGVTLV PIEEFSPEFV 

      1210       1220       1230       1240       1250       1260 
EPRVSCISSH GAFGPNSAAC LPSRFPKPPQ PIILRDCQVI PLPPGLPLTH AQDLTPAMSP 

      1270       1280       1290       1300       1310       1320 
AGPRPRPPTA VDPDAEPTLL REPQATVVFT THVPTLGRYA FLLHGYQPAH PTFPVEVLIN 

      1330       1340       1350       1360       1370       1380 
AGRVWQGHAN ASFCPHGYGC RTLVVCEGQA LLDVTHSELT VTVRVPKGRW LWLDYVLVVP 

      1390       1400       1410       1420       1430       1440 
ENVYSFGYLR EEPLDKSYDF ISHCAAQGYH ISPSSSSLFC RNAAASLSLF YNNGARPCGC 

      1450       1460       1470       1480       1490       1500 
HEVGATGPTC EPFGGQCPCH AHVIGRDCSR CATGYWGFPN CRPCDCGARL CDELTGQCIC 

      1510       1520       1530       1540       1550       1560 
PPRTIPPDCL LCQPQTFGCH PLVGCEECNC SGPGIQELTD PTCDTDSGQC KCRPNVTGRR 

      1570       1580       1590       1600       1610       1620 
CDTCSPGFHG YPRCRPCDCH EAGTAPGVCD PLTGQCYCKE NVQGPKCDQC SLGTFSLDAA 

      1630       1640       1650       1660       1670       1680 
NPKGCTRCFC FGATERCRSS SYTRQEFVDM EGWVLLSTDR QVVPHERQPG TEMLRADLRH 

      1690       1700       1710       1720       1730       1740 
VPEAVPEAFP ELYWQAPPSY LGDRVSSYGG TLRYELHSET QRGDVFVPME SRPDVVLQGN 

      1750       1760       1770       1780       1790       1800 
QMSITFLEPA YPTPGHVHRG QLQLVEGNFR HTETRNTVSR EELMMVLASL EQLQIRALFS 

      1810       1820       1830       1840       1850       1860 
QISSAVFLRR VALEVASPAG QGALASNVEL CLCPASYRGD SCQECAPGFY RDVKGLFLGR 

      1870       1880       1890       1900       1910       1920 
CVPCQCHGHS DRCLPGSGVC VDCQHNTEGA HCERCQAGFV SSRDDPSAPC VSCPCPLSVP 

      1930       1940       1950       1960       1970       1980 
SNNFAEGCVL RGGRTQCLCK PGYAGASCER CAPGFFGNPL VLGSSCQPCD CSGNGDPNLL 

      1990       2000       2010       2020       2030       2040 
FSDCDPLTGA CRGCLRHTTG PRCEICAPGF YGNALLPGNC TRCDCTPCGT EACDPHSGHC 

      2050       2060       2070       2080       2090       2100 
LCKAGVTGRR CDRCQEGHFG FDGCGGCRPC ACGPAAEGSE CHPQSGQCHC RPGTMGPQCR 

      2110       2120       2130       2140       2150       2160 
ECAPGYWGLP EQGCRRCQCP GGRCDPHTGR CNCPPGLSGE RCDTCSQQHQ VPVPGGPVGH 

      2170       2180       2190       2200       2210       2220 
SIHCEVCDHC VVLLLDDLER AGALLPAIHE QLRGINASSM AWARLHRLNA SIADLQSQLR 

      2230       2240       2250       2260       2270       2280 
SPLGPRHETA QQLEVLEQQS TSLGQDARRL GGQAVGTRDQ ASQLLAGTEA TLGHAKTLLA 

      2290       2300       2310       2320       2330       2340 
AIRAVDRTLS ELMSQTGHLG LANASAPSGE QLLRTLAEVE RLLWEMRARD LGAPQAAAEA 

      2350       2360       2370       2380       2390       2400 
ELAAAQRLLA RVQEQLSSLW EENQALATQT RDRLAQHEAG LMDLREALNR AVDATREAQE 

      2410       2420       2430       2440       2450       2460 
LNSRNQERLE EALQRKQELS RDNATLQATL HAARDTLASV FRLLHSLDQA KEELERLAAS 

      2470       2480       2490       2500       2510       2520 
LDGARTPLLQ RMQTFSPAGS KLRLVEAAEA HAQQLGQLAL NLSSIILDVN QDRLTQRAIE 

      2530       2540       2550       2560       2570       2580 
ASNAYSRILQ AVQAAEDAAG QALQQADHTW ATVVRQGLVD RAQQLLANST ALEEAMLQEQ 

      2590       2600       2610       2620       2630       2640 
QRLGLVWAAL QGARTQLRDV RAKKDQLEAH IQAAQAMLAM DTDETSKKIA HAKAVAAEAQ 

      2650       2660       2670       2680       2690       2700 
DTATRVQSQL QAMQENVERW QGQYEGLRGQ DLGQAVLDAG HSVSTLEKTL PQLLAKLSIL 

      2710       2720       2730       2740       2750       2760 
ENRGVHNASL ALSASIGRVR ELIAQARGAA SKVKVPMKFN GRSGVQLRTP RDLADLAAYT 

      2770       2780       2790       2800       2810       2820 
ALKFYLQGPE PEPGQGTEDR FVMYMGSRQA TGDYMGVSLR DKKVHWVYQL GEAGPAVLSI 

      2830       2840       2850       2860       2870       2880 
DEDIGEQFAA VSLDRTLQFG HMSVTVERQM IQETKGDTVA PGAEGLLNLR PDDFVFYVGG 

      2890       2900       2910       2920       2930       2940 
YPSTFTPPPL LRFPGYRGCI EMDTLNEEVV SLYNFERTFQ LDTAVDRPCA RSKSTGDPWL 

      2950       2960       2970       2980       2990       3000 
TDGSYLDGTG FARISFDSQI STTKRFEQEL RLVSYSGVLF FLKQQSQFLC LAVQEGSLVL 

      3010       3020       3030       3040       3050       3060 
LYDFGAGLKK AVPLQPPPPL TSASKAIQVF LLGGSRKRVL VRVERATVYS VEQDNDLELA 

      3070       3080       3090       3100       3110       3120 
DAYYLGGVPP DQLPPSLRRL FPTGGSVRGC VKGIKALGKY VDLKRLNTTG VSAGCTADLL 

      3130       3140       3150       3160       3170       3180 
VGRAMTFHGH GFLRLALSNV APLTGNVYSG FGFHSAQDSA LLYYRASPDG LCQVSLQQGR 

      3190       3200       3210       3220       3230       3240 
VSLQLLRTEV KTQAGFADGA PHYVAFYSNA TGVWLYVDDQ LQQMKPHRGP PPELQPQPEG 

      3250       3260       3270       3280       3290       3300 
PPRLLLGGLP ESGTIYNFSG CISNVFVQRL LGPQRVFDLQ QNLGSVNVST GCAPALQAQT 

      3310       3320       3330       3340       3350       3360 
PGLGPRGLQA TARKASRRSR QPARHPACML PPHLRTTRDS YQFGGSLSSH LEFVGILARH 

      3370       3380       3390       3400       3410       3420 
RNWPSLSMHV LPRSSRGLLL FTARLRPGSP SLALFLSNGH FVAQMEGLGT RLRAQSRQRS 

      3430       3440       3450       3460       3470       3480 
RPGRWHKVSV RWEKNRILLV TDGARAWSQE GPHRQHQGAE HPQPHTLFVG GLPASSHSSK 

      3490       3500       3510       3520       3530       3540 
LPVTVGFSGC VKRLRLHGRP LGAPTRMAGV TPCILGPLEA GLFFPGSGGV ITLDLPGATL 

      3550       3560       3570       3580       3590       3600 
PDVGLELEVR PLAVTGLIFH LGQARTPPYL QLQVTEKQVL LRADDGAGEF STSVTRPSVL 

      3610       3620       3630       3640       3650       3660 
CDGQWHRLAV MKSGNVLRLE VDAQSNHTVG PLLAAAAGAP APLYLGGLPE PMAVQPWPPA 

      3670       3680       3690 
YCGCMRRLAV NRSPVAMTRS VEVHGAVGAS GCPAA 

« Hide

References

« Hide 'large scale' references
[1]"Recombinant human laminin-10 (alpha5beta1gamma1). Production, purification, and migration-promoting activity on vascular endothelial cells."
Doi M., Thyboll J., Kortesmaa J., Jansson K., Iivanainen A., Parvardeh M., Timpl R., Hedin U., Swedenborg J., Tryggvason K.
J. Biol. Chem. 277:12741-12748(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-401; THR-1258; GLU-1367; SER-1807; MET-1900; ASN-2062 AND TRP-3079.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins."
Nagase T., Kikuno R., Ohara O.
DNA Res. 8:179-187(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1934, VARIANTS MET-889; GLU-1367 AND SER-1807.
Tissue: Brain.
[4]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2051-3695, VARIANTS ASN-2062 AND TRP-3079.
Tissue: Brain.
[5]"Tissue-specific expression of the human laminin alpha5-chain, and mapping of the gene to human chromosome 20q13.2-13.3 and to distal mouse chromosome 2 near the locus for the ragged (Ra) mutation."
Durkin M.E., Loechel F., Mattei M.-G., Gilpin B.J., Albrechtsen R., Wewer U.M.
FEBS Lett. 411:296-300(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2743-3695, VARIANT TRP-3079.
Tissue: Placenta.
[6]"Laminin expression in adult and developing retinae: evidence of two novel CNS laminins."
Libby R.T., Champliaud M.-F., Claudepierre T., Xu Y., Gibbons E.P., Koch M., Burgeson R.E., Hunter D.D., Brunken W.J.
J. Neurosci. 20:6517-6528(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: EXPRESSION IN RETINA.
[7]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2209; ASN-2303; ASN-2423; ASN-2501; ASN-2568; ASN-2707 AND ASN-3107.
Tissue: Liver.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF443072 mRNA. Translation: AAM12527.1.
AL354836 Genomic DNA. Translation: CAC22310.1. Sequence problems.
AB067494 mRNA. Translation: BAB67800.1.
AB011105 mRNA. Translation: BAA25459.1.
Z95636 mRNA. Translation: CAB09137.1.
CCDSCCDS33502.1.
RefSeqNP_005551.3. NM_005560.4.
UniGeneHs.473256.

3D structure databases

ProteinModelPortalO15230.
SMRO15230. Positions 42-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110105. 13 interactions.
IntActO15230. 11 interactions.
MINTMINT-1183475.
STRING9606.ENSP00000252999.

Chemistry

ChEMBLCHEMBL2364187.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteO15230.

Proteomic databases

MaxQBO15230.
PaxDbO15230.
PRIDEO15230.

Protocols and materials databases

DNASU3911.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252999; ENSP00000252999; ENSG00000130702.
GeneID3911.
KEGGhsa:3911.
UCSCuc002ycq.3. human.

Organism-specific databases

CTD3911.
GeneCardsGC20M060883.
H-InvDBHIX0015978.
HGNCHGNC:6485. LAMA5.
MIM601033. gene.
neXtProtNX_O15230.
PharmGKBPA30274.
HUGESearch...
Search...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292643.
HOGENOMHOG000231235.
HOVERGENHBG052300.
InParanoidO15230.
KOK06240.
OMAHTTGPRC.
PhylomeDBO15230.
TreeFamTF335359.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressO15230.
BgeeO15230.
CleanExHS_LAMA5.
GenevestigatorO15230.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR010307. Laminin_II.
IPR008211. Laminin_N.
IPR001368. TNFR/NGFR_Cys_rich_reg.
[Graphical view]
PfamPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 19 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 20 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 5 hits.
PROSITEPS00022. EGF_1. 19 hits.
PS01186. EGF_2. 3 hits.
PS01248. EGF_LAM_1. 19 hits.
PS50027. EGF_LAM_2. 21 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMA5. human.
GeneWikiLaminin,_alpha_5.
GenomeRNAi3911.
NextBio15363.
PROO15230.
SOURCESearch...

Entry information

Entry nameLAMA5_HUMAN
AccessionPrimary (citable) accession number: O15230
Secondary accession number(s): Q8TDF8, Q8WZA7, Q9H1P1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 150 of the entry and version 8 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM