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O15230

- LAMA5_HUMAN

UniProt

O15230 - LAMA5_HUMAN

Protein

Laminin subunit alpha-5

Gene

LAMA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 8 (11 Jan 2011)
      Previous versions | rss
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    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.

    GO - Molecular functioni

    1. integrin binding Source: UniProtKB
    2. structural molecule activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. branching involved in salivary gland morphogenesis Source: Ensembl
    3. branching involved in ureteric bud morphogenesis Source: Ensembl
    4. cell differentiation Source: UniProtKB
    5. cell migration Source: UniProtKB
    6. cell proliferation Source: UniProtKB
    7. cell recognition Source: UniProtKB
    8. cilium assembly Source: Ensembl
    9. cytoskeleton organization Source: UniProtKB
    10. embryo development Source: UniProtKB
    11. endothelial cell differentiation Source: UniProtKB
    12. establishment of protein localization to plasma membrane Source: Ensembl
    13. extracellular matrix disassembly Source: Reactome
    14. extracellular matrix organization Source: Reactome
    15. focal adhesion assembly Source: UniProtKB
    16. hair follicle development Source: Ensembl
    17. integrin-mediated signaling pathway Source: UniProtKB
    18. lung development Source: Ensembl
    19. morphogenesis of a polarized epithelium Source: Ensembl
    20. morphogenesis of embryonic epithelium Source: Ensembl
    21. muscle organ development Source: Ensembl
    22. neural crest cell migration Source: Ensembl
    23. odontogenesis of dentin-containing tooth Source: Ensembl
    24. regulation of cell adhesion Source: InterPro
    25. regulation of cell migration Source: InterPro
    26. regulation of cell proliferation Source: Ensembl
    27. regulation of embryonic development Source: InterPro
    28. substrate adhesion-dependent cell spreading Source: BHF-UCL

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit alpha-5
    Alternative name(s):
    Laminin-10 subunit alpha
    Laminin-11 subunit alpha
    Laminin-15 subunit alpha
    Gene namesi
    Name:LAMA5
    Synonyms:KIAA0533, KIAA1907
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:6485. LAMA5.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: UniProtKB
    2. basement membrane Source: UniProtKB
    3. extracellular region Source: Reactome
    4. extracellular space Source: UniProtKB
    5. extracellular vesicular exosome Source: UniProt
    6. laminin-10 complex Source: UniProtKB
    7. laminin-11 complex Source: BHF-UCL
    8. laminin-1 complex Source: InterPro
    9. laminin-5 complex Source: Ensembl
    10. nucleus Source: UniProt

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30274.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Sequence AnalysisAdd
    BLAST
    Chaini36 – 36953660Laminin subunit alpha-5PRO_0000017062Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi143 – 1431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi300 ↔ 309By similarity
    Disulfide bondi302 ↔ 322By similarity
    Disulfide bondi324 ↔ 333By similarity
    Disulfide bondi336 ↔ 356By similarity
    Disulfide bondi359 ↔ 368By similarity
    Disulfide bondi361 ↔ 393By similarity
    Disulfide bondi396 ↔ 405By similarity
    Disulfide bondi408 ↔ 426By similarity
    Disulfide bondi429 ↔ 440By similarity
    Disulfide bondi431 ↔ 447By similarity
    Disulfide bondi449 ↔ 458By similarity
    Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi461 ↔ 471By similarity
    Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi494 ↔ 506By similarity
    Disulfide bondi496 ↔ 515By similarity
    Disulfide bondi517 ↔ 526By similarity
    Disulfide bondi529 ↔ 538By similarity
    Disulfide bondi541 ↔ 553By similarity
    Disulfide bondi543 ↔ 560By similarity
    Disulfide bondi562 ↔ 571By similarity
    Disulfide bondi574 ↔ 584By similarity
    Disulfide bondi587 ↔ 599By similarity
    Disulfide bondi589 ↔ 605By similarity
    Disulfide bondi607 ↔ 616By similarity
    Disulfide bondi619 ↔ 629By similarity
    Disulfide bondi632 ↔ 644By similarity
    Disulfide bondi634 ↔ 650By similarity
    Disulfide bondi652 ↔ 661By similarity
    Disulfide bondi664 ↔ 674By similarity
    Disulfide bondi677 ↔ 689By similarity
    Disulfide bondi679 ↔ 696By similarity
    Disulfide bondi698 ↔ 707By similarity
    Disulfide bondi710 ↔ 725By similarity
    Disulfide bondi746 ↔ 755By similarity
    Disulfide bondi758 ↔ 773By similarity
    Disulfide bondi776 ↔ 790By similarity
    Disulfide bondi778 ↔ 797By similarity
    Disulfide bondi799 ↔ 808By similarity
    Disulfide bondi811 ↔ 826By similarity
    Disulfide bondi829 ↔ 841By similarity
    Disulfide bondi831 ↔ 848By similarity
    Disulfide bondi850 ↔ 859By similarity
    Glycosylationi900 – 9001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi921 – 9211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1330 – 13301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1438 ↔ 1450By similarity
    Disulfide bondi1440 ↔ 1457By similarity
    Disulfide bondi1459 ↔ 1468By similarity
    Disulfide bondi1471 ↔ 1481By similarity
    Disulfide bondi1484 ↔ 1491By similarity
    Disulfide bondi1486 ↔ 1498By similarity
    Disulfide bondi1500 ↔ 1509By similarity
    Disulfide bondi1512 ↔ 1525By similarity
    Disulfide bondi1528 ↔ 1543By similarity
    Glycosylationi1529 – 15291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1530 ↔ 1550By similarity
    Disulfide bondi1552 ↔ 1561By similarity
    Glycosylationi1555 – 15551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1564 ↔ 1574By similarity
    Disulfide bondi1577 ↔ 1589By similarity
    Disulfide bondi1579 ↔ 1596By similarity
    Disulfide bondi1598 ↔ 1607By similarity
    Disulfide bondi1610 ↔ 1625By similarity
    Disulfide bondi1864 ↔ 1873By similarity
    Disulfide bondi1866 ↔ 1880By similarity
    Disulfide bondi1883 ↔ 1892By similarity
    Disulfide bondi1895 ↔ 1910By similarity
    Disulfide bondi1913 ↔ 1928By similarity
    Disulfide bondi1915 ↔ 1937By similarity
    Disulfide bondi1939 ↔ 1948By similarity
    Disulfide bondi1951 ↔ 1966By similarity
    Disulfide bondi1969 ↔ 1984By similarity
    Disulfide bondi1971 ↔ 1991By similarity
    Disulfide bondi1994 ↔ 2003By similarity
    Disulfide bondi2006 ↔ 2020By similarity
    Disulfide bondi2023 ↔ 2033By similarity
    Disulfide bondi2025 ↔ 2040By similarity
    Disulfide bondi2042 ↔ 2051By similarity
    Disulfide bondi2054 ↔ 2067By similarity
    Disulfide bondi2070 ↔ 2081By similarity
    Disulfide bondi2072 ↔ 2088By similarity
    Disulfide bondi2090 ↔ 2099By similarity
    Disulfide bondi2102 ↔ 2114By similarity
    Disulfide bondi2117 ↔ 2124By similarity
    Disulfide bondi2119 ↔ 2131By similarity
    Disulfide bondi2133 ↔ 2142By similarity
    Disulfide bondi2145 ↔ 2164By similarity
    Disulfide bondi2167 – 2167InterchainCurated
    Disulfide bondi2170 – 2170InterchainCurated
    Glycosylationi2196 – 21961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2209 – 22091N-linked (GlcNAc...)1 Publication
    Glycosylationi2303 – 23031N-linked (GlcNAc...)1 Publication
    Glycosylationi2423 – 24231N-linked (GlcNAc...)1 Publication
    Glycosylationi2501 – 25011N-linked (GlcNAc...)1 Publication
    Glycosylationi2568 – 25681N-linked (GlcNAc...)1 Publication
    Glycosylationi2707 – 27071N-linked (GlcNAc...)1 Publication
    Disulfide bondi2899 ↔ 2929By similarity
    Disulfide bondi3090 ↔ 3115By similarity
    Glycosylationi3107 – 31071N-linked (GlcNAc...)1 Publication
    Glycosylationi3209 – 32091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3257 – 32571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3261 ↔ 3292By similarity
    Glycosylationi3287 – 32871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3490 ↔ 3513By similarity
    Glycosylationi3626 – 36261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3664 ↔ 3692By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO15230.
    PaxDbiO15230.
    PRIDEiO15230.

    PTM databases

    PhosphoSiteiO15230.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiO15230.
    BgeeiO15230.
    CleanExiHS_LAMA5.
    GenevestigatoriO15230.

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

    Protein-protein interaction databases

    BioGridi110105. 13 interactions.
    IntActiO15230. 12 interactions.
    MINTiMINT-1183475.
    STRINGi9606.ENSP00000252999.

    Structurei

    3D structure databases

    ProteinModelPortaliO15230.
    SMRiO15230. Positions 42-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 299259Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini300 – 35859Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini359 – 42870Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini429 – 47446Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini494 – 54047Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini541 – 58646Laminin EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini587 – 63145Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini632 – 67645Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini677 – 72246Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini723 – 77553Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini776 – 82853Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini829 – 85022Laminin EGF-like 11; truncatedPROSITE-ProRule annotationAdd
    BLAST
    Domaini1438 – 148346Laminin EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1484 – 152744Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1528 – 157649Laminin EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1577 – 162751Laminin EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1628 – 163710Laminin EGF-like 16; first partPROSITE-ProRule annotation
    Domaini1641 – 1830190Laminin IV type APROSITE-ProRule annotationAdd
    BLAST
    Domaini1831 – 186333Laminin EGF-like 16; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1864 – 191249Laminin EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini1913 – 196856Laminin EGF-like 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini1969 – 202254Laminin EGF-like 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2023 – 206947Laminin EGF-like 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2070 – 211647Laminin EGF-like 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini2117 – 216650Laminin EGF-like 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini2736 – 2929194Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2941 – 3115175Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini3124 – 3292169Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini3340 – 3513174Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini3520 – 3692173Laminin G-like 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni851 – 1437587Domain IV 1 (domain IV B)Add
    BLAST
    Regioni2167 – 2735569Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili2203 – 222119Sequence AnalysisAdd
    BLAST
    Coiled coili2335 – 2466132Sequence AnalysisAdd
    BLAST
    Coiled coili2510 – 2670161Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1722 – 17243Cell attachment siteSequence Analysis
    Motifi1838 – 18403Cell attachment siteSequence Analysis

    Domaini

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

    Sequence similaritiesi

    Contains 22 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 5 laminin G-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

    eggNOGiNOG292643.
    HOGENOMiHOG000231235.
    HOVERGENiHBG052300.
    InParanoidiO15230.
    KOiK06240.
    OMAiHTTGPRC.
    PhylomeDBiO15230.
    TreeFamiTF335359.

    Family and domain databases

    Gene3Di2.60.120.200. 5 hits.
    InterProiIPR008985. 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]
    PfamiPF00052. 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]
    SMARTiSM00180. EGF_Lam. 20 hits.
    SM00281. LamB. 1 hit.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 5 hits.
    PROSITEiPS00022. 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]

    Sequencei

    Sequence statusi: Complete.

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

    O15230-1 [UniParc]FASTAAdd to Basket

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    MAKRLCAGSA LCVRGPRGPA PLLLVGLALL GAARAREEAG GGFSLHPPYF     50
    NLAEGARIAA SATCGEEAPA RGSPRPTEDL YCKLVGGPVA GGDPNQTIRG 100
    QYCDICTAAN SNKAHPASNA IDGTERWWQS PPLSRGLEYN EVNVTLDLGQ 150
    VFHVAYVLIK FANSPRPDLW VLERSMDFGR TYQPWQFFAS SKRDCLERFG 200
    PQTLERITRD DAAICTTEYS RIVPLENGEI VVSLVNGRPG AMNFSYSPLL 250
    REFTKATNVR LRFLRTNTLL GHLMGKALRD PTVTRRYYYS IKDISIGGRC 300
    VCHGHADACD AKDPTDPFRL QCTCQHNTCG GTCDRCCPGF NQQPWKPATA 350
    NSANECQSCN CYGHATDCYY DPEVDRRRAS QSLDGTYQGG GVCIDCQHHT 400
    TGVNCERCLP GFYRSPNHPL DSPHVCRRCN CESDFTDGTC EDLTGRCYCR 450
    PNFSGERCDV CAEGFTGFPS CYPTPSSSND TREQVLPAGQ IVNCDCSAAG 500
    TQGNACRKDP RVGRCLCKPN FQGTHCELCA PGFYGPGCQP CQCSSPGVAD 550
    DRCDPDTGQC RCRVGFEGAT CDRCAPGYFH FPLCQLCGCS PAGTLPEGCD 600
    EAGRCLCQPE FAGPHCDRCR PGYHGFPNCQ ACTCDPRGAL DQLCGAGGLC 650
    RCRPGYTGTA CQECSPGFHG FPSCVPCHCS AEGSLHAACD PRSGQCSCRP 700
    RVTGLRCDTC VPGAYNFPYC EAGSCHPAGL APVDPALPEA QVPCMCRAHV 750
    EGPSCDRCKP GFWGLSPSNP EGCTRCSCDL RGTLGGVAEC QPGTGQCFCK 800
    PHVCGQACAS CKDGFFGLDQ ADYFGCRSCR CDIGGALGQS CEPRTGVCRC 850
    RPNTQGPTCS EPARDHYLPD LHHLRLELEE AATPEGHAVR FGFNPLEFEN 900
    FSWRGYAQMA PVQPRIVARL NLTSPDLFWL VFRYVNRGAM SVSGRVSVRE 950
    EGRSATCANC TAQSQPVAFP PSTEPAFITV PQRGFGEPFV LNPGTWALRV 1000
    EAEGVLLDYV VLLPSAYYEA ALLQLRVTEA CTYRPSAQQS GDNCLLYTHL 1050
    PLDGFPSAAG LEALCRQDNS LPRPCPTEQL SPSHPPLITC TGSDVDVQLQ 1100
    VAVPQPGRYA LVVEYANEDA RQEVGVAVHT PQRAPQQGLL SLHPCLYSTL 1150
    CRGTARDTQD HLAVFHLDSE ASVRLTAEQA RFFLHGVTLV PIEEFSPEFV 1200
    EPRVSCISSH GAFGPNSAAC LPSRFPKPPQ PIILRDCQVI PLPPGLPLTH 1250
    AQDLTPAMSP AGPRPRPPTA VDPDAEPTLL REPQATVVFT THVPTLGRYA 1300
    FLLHGYQPAH PTFPVEVLIN AGRVWQGHAN ASFCPHGYGC RTLVVCEGQA 1350
    LLDVTHSELT VTVRVPKGRW LWLDYVLVVP ENVYSFGYLR EEPLDKSYDF 1400
    ISHCAAQGYH ISPSSSSLFC RNAAASLSLF YNNGARPCGC HEVGATGPTC 1450
    EPFGGQCPCH AHVIGRDCSR CATGYWGFPN CRPCDCGARL CDELTGQCIC 1500
    PPRTIPPDCL LCQPQTFGCH PLVGCEECNC SGPGIQELTD PTCDTDSGQC 1550
    KCRPNVTGRR CDTCSPGFHG YPRCRPCDCH EAGTAPGVCD PLTGQCYCKE 1600
    NVQGPKCDQC SLGTFSLDAA NPKGCTRCFC FGATERCRSS SYTRQEFVDM 1650
    EGWVLLSTDR QVVPHERQPG TEMLRADLRH VPEAVPEAFP ELYWQAPPSY 1700
    LGDRVSSYGG TLRYELHSET QRGDVFVPME SRPDVVLQGN QMSITFLEPA 1750
    YPTPGHVHRG QLQLVEGNFR HTETRNTVSR EELMMVLASL EQLQIRALFS 1800
    QISSAVFLRR VALEVASPAG QGALASNVEL CLCPASYRGD SCQECAPGFY 1850
    RDVKGLFLGR CVPCQCHGHS DRCLPGSGVC VDCQHNTEGA HCERCQAGFV 1900
    SSRDDPSAPC VSCPCPLSVP SNNFAEGCVL RGGRTQCLCK PGYAGASCER 1950
    CAPGFFGNPL VLGSSCQPCD CSGNGDPNLL FSDCDPLTGA CRGCLRHTTG 2000
    PRCEICAPGF YGNALLPGNC TRCDCTPCGT EACDPHSGHC LCKAGVTGRR 2050
    CDRCQEGHFG FDGCGGCRPC ACGPAAEGSE CHPQSGQCHC RPGTMGPQCR 2100
    ECAPGYWGLP EQGCRRCQCP GGRCDPHTGR CNCPPGLSGE RCDTCSQQHQ 2150
    VPVPGGPVGH SIHCEVCDHC VVLLLDDLER AGALLPAIHE QLRGINASSM 2200
    AWARLHRLNA SIADLQSQLR SPLGPRHETA QQLEVLEQQS TSLGQDARRL 2250
    GGQAVGTRDQ ASQLLAGTEA TLGHAKTLLA AIRAVDRTLS ELMSQTGHLG 2300
    LANASAPSGE QLLRTLAEVE RLLWEMRARD LGAPQAAAEA ELAAAQRLLA 2350
    RVQEQLSSLW EENQALATQT RDRLAQHEAG LMDLREALNR AVDATREAQE 2400
    LNSRNQERLE EALQRKQELS RDNATLQATL HAARDTLASV FRLLHSLDQA 2450
    KEELERLAAS LDGARTPLLQ RMQTFSPAGS KLRLVEAAEA HAQQLGQLAL 2500
    NLSSIILDVN QDRLTQRAIE ASNAYSRILQ AVQAAEDAAG QALQQADHTW 2550
    ATVVRQGLVD RAQQLLANST ALEEAMLQEQ QRLGLVWAAL QGARTQLRDV 2600
    RAKKDQLEAH IQAAQAMLAM DTDETSKKIA HAKAVAAEAQ DTATRVQSQL 2650
    QAMQENVERW QGQYEGLRGQ DLGQAVLDAG HSVSTLEKTL PQLLAKLSIL 2700
    ENRGVHNASL ALSASIGRVR ELIAQARGAA SKVKVPMKFN GRSGVQLRTP 2750
    RDLADLAAYT ALKFYLQGPE PEPGQGTEDR FVMYMGSRQA TGDYMGVSLR 2800
    DKKVHWVYQL GEAGPAVLSI DEDIGEQFAA VSLDRTLQFG HMSVTVERQM 2850
    IQETKGDTVA PGAEGLLNLR PDDFVFYVGG YPSTFTPPPL LRFPGYRGCI 2900
    EMDTLNEEVV SLYNFERTFQ LDTAVDRPCA RSKSTGDPWL TDGSYLDGTG 2950
    FARISFDSQI STTKRFEQEL RLVSYSGVLF FLKQQSQFLC LAVQEGSLVL 3000
    LYDFGAGLKK AVPLQPPPPL TSASKAIQVF LLGGSRKRVL VRVERATVYS 3050
    VEQDNDLELA DAYYLGGVPP DQLPPSLRRL FPTGGSVRGC VKGIKALGKY 3100
    VDLKRLNTTG VSAGCTADLL VGRAMTFHGH GFLRLALSNV APLTGNVYSG 3150
    FGFHSAQDSA LLYYRASPDG LCQVSLQQGR VSLQLLRTEV KTQAGFADGA 3200
    PHYVAFYSNA TGVWLYVDDQ LQQMKPHRGP PPELQPQPEG PPRLLLGGLP 3250
    ESGTIYNFSG CISNVFVQRL LGPQRVFDLQ QNLGSVNVST GCAPALQAQT 3300
    PGLGPRGLQA TARKASRRSR QPARHPACML PPHLRTTRDS YQFGGSLSSH 3350
    LEFVGILARH RNWPSLSMHV LPRSSRGLLL FTARLRPGSP SLALFLSNGH 3400
    FVAQMEGLGT RLRAQSRQRS RPGRWHKVSV RWEKNRILLV TDGARAWSQE 3450
    GPHRQHQGAE HPQPHTLFVG GLPASSHSSK LPVTVGFSGC VKRLRLHGRP 3500
    LGAPTRMAGV TPCILGPLEA GLFFPGSGGV ITLDLPGATL PDVGLELEVR 3550
    PLAVTGLIFH LGQARTPPYL QLQVTEKQVL LRADDGAGEF STSVTRPSVL 3600
    CDGQWHRLAV MKSGNVLRLE VDAQSNHTVG PLLAAAAGAP APLYLGGLPE 3650
    PMAVQPWPPA YCGCMRRLAV NRSPVAMTRS VEVHGAVGAS GCPAA 3695
    Length:3,695
    Mass (Da):399,737
    Last modified:January 11, 2011 - v8
    Checksum:iB13C479B55282E3C
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti956 – 9561T → A in AAM12527. (PubMed:11821406)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti401 – 4011T → A.1 Publication
    Corresponds to variant rs4925229 [ dbSNP | Ensembl ].
    VAR_047887
    Natural varianti889 – 8891V → M.1 Publication
    Corresponds to variant rs6062223 [ dbSNP | Ensembl ].
    VAR_030847
    Natural varianti1258 – 12581M → T.1 Publication
    Corresponds to variant rs3810548 [ dbSNP | Ensembl ].
    VAR_030848
    Natural varianti1367 – 13671K → E.2 Publications
    Corresponds to variant rs2427286 [ dbSNP | Ensembl ].
    VAR_030849
    Natural varianti1434 – 14341G → A.
    Corresponds to variant rs17750870 [ dbSNP | Ensembl ].
    VAR_030850
    Natural varianti1667 – 16671R → W.
    Corresponds to variant rs13039398 [ dbSNP | Ensembl ].
    VAR_030851
    Natural varianti1671 – 16711T → M.
    Corresponds to variant rs944893 [ dbSNP | Ensembl ].
    VAR_047888
    Natural varianti1717 – 17171H → Y.
    Corresponds to variant rs875379 [ dbSNP | Ensembl ].
    VAR_030852
    Natural varianti1807 – 18071F → S.2 Publications
    Corresponds to variant rs2427284 [ dbSNP | Ensembl ].
    VAR_030853
    Natural varianti1900 – 19001V → M.1 Publication
    Corresponds to variant rs2427283 [ dbSNP | Ensembl ].
    VAR_030854
    Natural varianti1908 – 19081A → T.
    Corresponds to variant rs11698080 [ dbSNP | Ensembl ].
    VAR_030855
    Natural varianti2036 – 20361H → R.
    Corresponds to variant rs6143021 [ dbSNP | Ensembl ].
    VAR_030856
    Natural varianti2053 – 20531R → H.
    Corresponds to variant rs3737137 [ dbSNP | Ensembl ].
    VAR_030857
    Natural varianti2062 – 20621D → N.2 Publications
    Corresponds to variant rs2274934 [ dbSNP | Ensembl ].
    VAR_030858
    Natural varianti2226 – 22261R → H.
    Corresponds to variant rs2297587 [ dbSNP | Ensembl ].
    VAR_030859
    Natural varianti3079 – 30791R → W.3 Publications
    Corresponds to variant rs944895 [ dbSNP | Ensembl ].
    VAR_030860

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS33502.1.
    RefSeqiNP_005551.3. NM_005560.4.
    UniGeneiHs.473256.

    Genome annotation databases

    EnsembliENST00000252999; ENSP00000252999; ENSG00000130702.
    GeneIDi3911.
    KEGGihsa:3911.
    UCSCiuc002ycq.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS33502.1.
    RefSeqi NP_005551.3. NM_005560.4.
    UniGenei Hs.473256.

    3D structure databases

    ProteinModelPortali O15230.
    SMRi O15230. Positions 42-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110105. 13 interactions.
    IntActi O15230. 12 interactions.
    MINTi MINT-1183475.
    STRINGi 9606.ENSP00000252999.

    Chemistry

    ChEMBLi CHEMBL2364187.
    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00015. Reteplase.
    DB00031. Tenecteplase.

    PTM databases

    PhosphoSitei O15230.

    Proteomic databases

    MaxQBi O15230.
    PaxDbi O15230.
    PRIDEi O15230.

    Protocols and materials databases

    DNASUi 3911.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252999 ; ENSP00000252999 ; ENSG00000130702 .
    GeneIDi 3911.
    KEGGi hsa:3911.
    UCSCi uc002ycq.3. human.

    Organism-specific databases

    CTDi 3911.
    GeneCardsi GC20M060883.
    H-InvDB HIX0015978.
    HGNCi HGNC:6485. LAMA5.
    MIMi 601033. gene.
    neXtProti NX_O15230.
    PharmGKBi PA30274.
    HUGEi Search...
    Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292643.
    HOGENOMi HOG000231235.
    HOVERGENi HBG052300.
    InParanoidi O15230.
    KOi K06240.
    OMAi HTTGPRC.
    PhylomeDBi O15230.
    TreeFami TF335359.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.

    Miscellaneous databases

    ChiTaRSi LAMA5. human.
    GeneWikii Laminin,_alpha_5.
    GenomeRNAii 3911.
    NextBioi 15363.
    PROi O15230.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15230.
    Bgeei O15230.
    CleanExi HS_LAMA5.
    Genevestigatori O15230.

    Family and domain databases

    Gene3Di 2.60.120.200. 5 hits.
    InterProi IPR008985. 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 ]
    Pfami PF00052. 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 ]
    SMARTi SM00180. EGF_Lam. 20 hits.
    SM00281. LamB. 1 hit.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 5 hits.
    PROSITEi PS00022. 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLAMA5_HUMAN
    AccessioniPrimary (citable) accession number: O15230
    Secondary accession number(s): Q8TDF8, Q8WZA7, Q9H1P1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 152 of the entry and version 8 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3