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Q16787

- LAMA3_HUMAN

UniProt

Q16787 - LAMA3_HUMAN

Protein

Laminin subunit alpha-3

Gene

LAMA3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      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.
    Laminin-5 is thought to be involved in (1) cell adhesion via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine phosphorylation of pp125-FAK and p80, (3) differentiation of keratinocytes.

    GO - Molecular functioni

    1. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. cell junction assembly Source: Reactome
    3. epidermis development Source: ProtInc
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. hemidesmosome assembly Source: Reactome
    7. regulation of cell adhesion Source: InterPro
    8. regulation of cell migration Source: InterPro
    9. regulation of embryonic development Source: InterPro

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150268. Anchoring fibril formation.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.
    REACT_20537. Type I hemidesmosome assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit alpha-3
    Alternative name(s):
    Epiligrin 170 kDa subunit
    Short name:
    E170
    Epiligrin subunit alpha
    Kalinin subunit alpha
    Laminin-5 subunit alpha
    Laminin-6 subunit alpha
    Laminin-7 subunit alpha
    Nicein subunit alpha
    Gene namesi
    Name:LAMA3
    Synonyms:LAMNA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6483. LAMA3.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: ProtInc
    2. extracellular region Source: Reactome
    3. laminin-1 complex Source: InterPro
    4. laminin-5 complex Source: Ensembl

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Laryngoonychocutaneous syndrome (LOCS) [MIM:245660]: Autosomal recessive epithelial disorder confined to the Punjabi Muslim population. The condition is characterized by cutaneous erosions, nail dystrophy and exuberant vascular granulation tissue in certain epithelia, especially conjunctiva and larynx.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Epidermolysis bullosa

    Organism-specific databases

    MIMi226700. phenotype.
    245660. phenotype.
    Orphaneti79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
    79404. Junctional epidermolysis bullosa, Herlitz type.
    2407. LOC syndrome.
    PharmGKBiPA30272.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Sequence AnalysisAdd
    BLAST
    Chaini36 – 33333298Laminin subunit alpha-3PRO_0000017058Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi299 ↔ 308By similarity
    Disulfide bondi301 ↔ 319By similarity
    Disulfide bondi321 ↔ 330By similarity
    Disulfide bondi333 ↔ 353By similarity
    Disulfide bondi356 ↔ 365By similarity
    Disulfide bondi358 ↔ 390By similarity
    Disulfide bondi393 ↔ 402By similarity
    Disulfide bondi405 ↔ 423By similarity
    Disulfide bondi426 ↔ 436By similarity
    Disulfide bondi428 ↔ 443By similarity
    Disulfide bondi445 ↔ 454By similarity
    Disulfide bondi457 ↔ 467By similarity
    Disulfide bondi491 ↔ 503By similarity
    Disulfide bondi493 ↔ 509By similarity
    Disulfide bondi511 ↔ 520By similarity
    Disulfide bondi523 ↔ 533By similarity
    Disulfide bondi536 ↔ 548By similarity
    Disulfide bondi538 ↔ 555By similarity
    Disulfide bondi557 ↔ 566By similarity
    Disulfide bondi569 ↔ 586By similarity
    Disulfide bondi601 ↔ 610By similarity
    Disulfide bondi613 ↔ 628By similarity
    Disulfide bondi631 ↔ 645By similarity
    Disulfide bondi633 ↔ 652By similarity
    Disulfide bondi654 ↔ 663By similarity
    Disulfide bondi666 ↔ 681By similarity
    Disulfide bondi684 ↔ 696By similarity
    Disulfide bondi686 ↔ 703By similarity
    Disulfide bondi705 ↔ 714By similarity
    Disulfide bondi1266 ↔ 1278By similarity
    Disulfide bondi1268 ↔ 1285By similarity
    Disulfide bondi1287 ↔ 1296By similarity
    Disulfide bondi1299 ↔ 1309By similarity
    Disulfide bondi1312 ↔ 1319By similarity
    Disulfide bondi1314 ↔ 1326By similarity
    Disulfide bondi1328 ↔ 1337By similarity
    Disulfide bondi1340 ↔ 1353By similarity
    Disulfide bondi1356 ↔ 1371By similarity
    Disulfide bondi1358 ↔ 1378By similarity
    Disulfide bondi1380 ↔ 1389By similarity
    Disulfide bondi1392 ↔ 1402By similarity
    Disulfide bondi1405 ↔ 1417By similarity
    Disulfide bondi1407 ↔ 1424By similarity
    Disulfide bondi1426 ↔ 1435By similarity
    Disulfide bondi1438 ↔ 1453By similarity
    Disulfide bondi1687 ↔ 1696By similarity
    Disulfide bondi1689 ↔ 1703By similarity
    Disulfide bondi1706 ↔ 1715By similarity
    Disulfide bondi1718 ↔ 1731By similarity
    Disulfide bondi1734 ↔ 1746By similarity
    Disulfide bondi1736 ↔ 1755By similarity
    Disulfide bondi1757 ↔ 1766By similarity
    Disulfide bondi1769 ↔ 1784By similarity
    Disulfide bondi1822 – 1822InterchainCurated
    Disulfide bondi1825 – 1825InterchainCurated
    Glycosylationi2365 – 23651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2502 – 25021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2561 ↔ 2591By similarity
    Glycosylationi2584 – 25841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2737 ↔ 2760By similarity
    Disulfide bondi2895 ↔ 2927By similarity
    Disulfide bondi3127 ↔ 3150By similarity
    Disulfide bondi3302 ↔ 3330By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ16787.
    PaxDbiQ16787.
    PRIDEiQ16787.

    PTM databases

    PhosphoSiteiQ16787.

    Miscellaneous databases

    PMAP-CutDBQ6VU68.

    Expressioni

    Tissue specificityi

    Skin; respiratory, urinary, and digestive epithelia and in other specialized tissues with prominent secretory or protective functions. Epithelial basement membrane, and epithelial cell tongue that migrates into a wound bed. A differential and focal expression of the subunit alpha-3 is observed in the CNS.

    Inductioni

    Laminin-5 is up-regulated in wound sites of human skin.

    Gene expression databases

    ArrayExpressiQ16787.
    BgeeiQ16787.
    CleanExiHS_LAMA3.
    GenevestigatoriQ16787.

    Organism-specific databases

    HPAiCAB010757.
    HPA009309.

    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-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin) and laminin-7 (laminin-321 or KS-laminin).

    Protein-protein interaction databases

    BioGridi110103. 4 interactions.
    IntActiQ16787. 3 interactions.
    MINTiMINT-1431248.
    STRINGi9606.ENSP00000324532.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16787.
    SMRiQ16787. Positions 44-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 298256Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini299 – 35557Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini356 – 42570Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini426 – 46944Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini491 – 53545Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini536 – 58853Laminin EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini590 – 63041Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini631 – 68353Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini684 – 72845Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1266 – 131146Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1312 – 135544Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1356 – 140449Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1405 – 145551Laminin EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1476 – 1653178Laminin IV type APROSITE-ProRule annotationAdd
    BLAST
    Domaini1687 – 173347Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1734 – 178653Laminin EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1787 – 182135Laminin EGF-like 15; truncatedPROSITE-ProRule annotationAdd
    BLAST
    Domaini2390 – 2591202Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2598 – 2760163Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2767 – 2927161Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini2986 – 3150165Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini3157 – 3330174Laminin G-like 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni298 – 728431Domain VAdd
    BLAST
    Regioni796 – 1265470Domain IV 1 (domain IV B)Add
    BLAST
    Regioni1266 – 1465200Domain III BAdd
    BLAST
    Regioni1654 – 1821168Domain III AAdd
    BLAST
    Regioni1822 – 2389568Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1852 – 194190Sequence AnalysisAdd
    BLAST
    Coiled coili1987 – 2169183Sequence AnalysisAdd
    BLAST
    Coiled coili2322 – 238867Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2278 – 22803Cell attachment siteSequence Analysis

    Domaini

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

    Sequence similaritiesi

    Contains 15 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.
    KOiK06240.
    OMAiRGLYFTE.
    OrthoDBiEOG7DFXB9.
    PhylomeDBiQ16787.
    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.
    [Graphical view]
    PfamiPF00052. Laminin_B. 1 hit.
    PF00053. Laminin_EGF. 12 hits.
    PF00054. Laminin_G_1. 1 hit.
    PF02210. Laminin_G_2. 4 hits.
    PF06008. Laminin_I. 1 hit.
    PF06009. Laminin_II. 1 hit.
    PF00055. Laminin_N. 1 hit.
    [Graphical view]
    SMARTiSM00180. EGF_Lam. 14 hits.
    SM00281. LamB. 1 hit.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 5 hits.
    PROSITEiPS00022. EGF_1. 12 hits.
    PS01186. EGF_2. 1 hit.
    PS01248. EGF_LAM_1. 13 hits.
    PS50027. EGF_LAM_2. 14 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    PS51115. LAMININ_IVA. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q16787-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAAARPRGR ALGPVLPPTP LLLLVLRVLP ACGATARDPG AAAGLSLHPT     50
    YFNLAEAARI WATATCGERG PGEGRPQPEL YCKLVGGPTA PGSGHTIQGQ 100
    FCDYCNSEDP RKAHPVTNAI DGSERWWQSP PLSSGTQYNR VNLTLDLGQL 150
    FHVAYILIKF ANSPRPDLWV LERSVDFGST YSPWQYFAHS KVDCLKEFGR 200
    EANMAVTRDD DVLCVTEYSR IVPLENGEVV VSLINGRPGA KNFTFSHTLR 250
    EFTKATNIRL RFLRTNTLLG HLISKAQRDP TVTRRYYYSI KDISIGGQCV 300
    CNGHAEVCNI NNPEKLFRCE CQHHTCGETC DRCCTGYNQR RWRPAAWEQS 350
    HECEACNCHG HASNCYYDPD VERQQASLNT QGIYAGGGVC INCQHNTAGV 400
    NCEQCAKGYY RPYGVPVDAP DGCIPCSCDP EHADGCEQGS GRCHCKPNFH 450
    GDNCEKCAIG YYNFPFCLRI PIFPVSTPSS EDPVAGDIKG CDCNLEGVLP 500
    EICDAHGRCL CRPGVEGPRC DTCRSGFYSF PICQACWCSA LGSYQMPCSS 550
    VTGQCECRPG VTGQRCDRCL SGAYDFPHCQ GSSSACDPAG TINSNLGYCQ 600
    CKLHVEGPTC SRCKLLYWNL DKENPSGCSE CKCHKAGTVS GTGECRQGDG 650
    DCHCKSHVGG DSCDTCEDGY FALEKSNYFG CQGCQCDIGG ALSSMCSGPS 700
    GVCQCREHVV GKVCQRPENN YYFPDLHHMK YEIEDGSTPN GRDLRFGFDP 750
    LAFPEFSWRG YAQMTSVQND VRITLNVGKS SGSLFRVILR YVNPGTEAVS 800
    GHITIYPSWG AAQSKEIIFL PSKEPAFVTV PGNGFADPFS ITPGIWVACI 850
    KAEGVLLDYL VLLPRDYYEA SVLQLPVTEP CAYAGPPQEN CLLYQHLPVT 900
    RFPCTLACEA RHFLLDGEPR PVAVRQPTPA HPVMVDLSGR EVELHLRLRI 950
    PQVGHYVVVV EYSTEAAQLF VVDVNVKSSG SVLAGQVNIY SCNYSVLCRS 1000
    AVIDHMSRIA MYELLADADI QLKGHMARFL LHQVCIIPIE EFSAEYVRPQ 1050
    VHCIASYGRF VNQSATCVSL AHETPPTALI LDVLSGRPFP HLPQQSSPSV 1100
    DVLPGVTLKA PQNQVTLRGR VPHLGRYVFV IHFYQAAHPT FPAQVSVDGG 1150
    WPRAGSFHAS FCPHVLGCRD QVIAEGQIEF DISEPEVAAT VKVPEGKSLV 1200
    LVRVLVVPAE NYDYQILHKK SMDKSLEFIT NCGKNSFYLD PQTASRFCKN 1250
    SARSLVAFYH KGALPCECHP TGATGPHCSP EGGQCPCQPN VIGRQCTRCA 1300
    TGHYGFPRCK PCSCGRRLCE EMTGQCRCPP RTVRPQCEVC ETHSFSFHPM 1350
    AGCEGCNCSR RGTIEAAMPE CDRDSGQCRC KPRITGRQCD RCASGFYRFP 1400
    ECVPCNCNRD GTEPGVCDPG TGACLCKENV EGTECNVCRE GSFHLDPANL 1450
    KGCTSCFCFG VNNQCHSSHK RRTKFVDMLG WHLETADRVD IPVSFNPGSN 1500
    SMVADLQELP ATIHSASWVA PTSYLGDKVS SYGGYLTYQA KSFGLPGDMV 1550
    LLEKKPDVQL TGQHMSIIYE ETNTPRPDRL HHGRVHVVEG NFRHASSRAP 1600
    VSREELMTVL SRLADVRIQG LYFTETQRLT LSEVGLEEAS DTGSGRIALA 1650
    VEICACPPAY AGDSCQGCSP GYYRDHKGLY TGRCVPCNCN GHSNQCQDGS 1700
    GICVNCQHNT AGEHCERCQE GYYGNAVHGS CRACPCPHTN SFATGCVVNG 1750
    GDVRCSCKAG YTGTQCERCA PGYFGNPQKF GGSCQPCSCN SNGQLGSCHP 1800
    LTGDCINQEP KDSSPAEECD DCDSCVMTLL NDLATMGEQL RLVKSQLQGL 1850
    SASAGLLEQM RHMETQAKDL RNQLLNYRSA ISNHGSKIEG LERELTDLNQ 1900
    EFETLQEKAQ VNSRKAQTLN NNVNRATQSA KELDVKIKNV IRNVHILLKQ 1950
    ISGTDGEGNN VPSGDFSREW AEAQRMMREL RNRNFGKHLR EAEADKRESQ 2000
    LLLNRIRTWQ KTHQGENNGL ANSIRDSLNE YEAKLSDLRA RLQEAAAQAK 2050
    QANGLNQENE RALGAIQRQV KEINSLQSDF TKYLTTADSS LLQTNIALQL 2100
    MEKSQKEYEK LAASLNEARQ ELSDKVRELS RSAGKTSLVE EAEKHARSLQ 2150
    ELAKQLEEIK RNASGDELVR CAVDAATAYE NILNAIKAAE DAANRAASAS 2200
    ESALQTVIKE DLPRKAKTLS SNSDKLLNEA KMTQKKLKQE VSPALNNLQQ 2250
    TLNIVTVQKE VIDTNLTTLR DGLHGIQRGD IDAMISSAKS MVRKANDITD 2300
    EVLDGLNPIQ TDVERIKDTY GRTQNEDFKK ALTDADNSVN KLTNKLPDLW 2350
    RKIESINQQL LPLGNISDNM DRIRELIQQA RDAASKVAVP MRFNGKSGVE 2400
    VRLPNDLEDL KGYTSLSLFL QRPNSRENGG TENMFVMYLG NKDASRDYIG 2450
    MAVVDGQLTC VYNLGDREAE LQVDQILTKS ETKEAVMDRV KFQRIYQFAR 2500
    LNYTKGATSS KPETPGVYDM DGRNSNTLLN LDPENVVFYV GGYPPDFKLP 2550
    SRLSFPPYKG CIELDDLNEN VLSLYNFKKT FNLNTTEVEP CRRRKEESDK 2600
    NYFEGTGYAR VPTQPHAPIP TFGQTIQTTV DRGLLFFAEN GDRFISLNIE 2650
    DGKLMVRYKL NSELPKERGV GDAINNGRDH SIQIKIGKLQ KRMWINVDVQ 2700
    NTIIDGEVFD FSTYYLGGIP IAIRERFNIS TPAFRGCMKN LKKTSGVVRL 2750
    NDTVGVTKKC SEDWKLVRSA SFSRGGQLSF TDLGLPPTDH LQASFGFQTF 2800
    QPSGILLDHQ TWTRNLQVTL EDGYIELSTS DSGSPIFKSP QTYMDGLLHY 2850
    VSVISDNSGL RLLIDDQLLR NSKRLKHISS SRQSLRLGGS NFEGCISNVF 2900
    VQRLSLSPEV LDLTSNSLKR DVSLGGCSLN KPPFLMLLKG STRFNKTKTF 2950
    RINQLLQDTP VASPRSVKVW QDACSPLPKT QANHGALQFG DIPTSHLLFK 3000
    LPQELLKPRS QFAVDMQTTS SRGLVFHTGT KNSFMALYLS KGRLVFALGT 3050
    DGKKLRIKSK EKCNDGKWHT VVFGHDGEKG RLVVDGLRAR EGSLPGNSTI 3100
    SIRAPVYLGS PPSGKPKSLP TNSFVGCLKN FQLDSKPLYT PSSSFGVSSC 3150
    LGGPLEKGIY FSEEGGHVVL AHSVLLGPEF KLVFSIRPRS LTGILIHIGS 3200
    QPGKHLCVYL EAGKVTASMD SGAGGTSTSV TPKQSLCDGQ WHSVAVTIKQ 3250
    HILHLELDTD SSYTAGQIPF PPASTQEPLH LGGAPANLTT LRIPVWKSFF 3300
    GCLRNIHVNH IPVPVTEALE VQGPVSLNGC PDQ 3333
    Length:3,333
    Mass (Da):366,649
    Last modified:November 25, 2008 - v2
    Checksum:i9F99AF49B8EF27DD
    GO
    Isoform 1 (identifier: Q16787-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1620: Missing.
         1621-1665: LYFTETQRLT...CPPAYAGDSC → MPPAVRRSAC...QASYVEFRPS

    Show »
    Length:1,724
    Mass (Da):190,491
    Checksum:i0477C729951763A5
    GO
    Isoform 3 (identifier: Q16787-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1946-2002: ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLL → M

    Show »
    Length:3,277
    Mass (Da):360,212
    Checksum:i3ACFFE998357122E
    GO
    Isoform 4 (identifier: Q16787-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1609: Missing.
         1610-1665: LSRLADVRIQ...CPPAYAGDSC → MPPAVRRSAC...QASYVEFRPS
         1946-2002: ILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLL → M

    Show »
    Length:1,668
    Mass (Da):184,054
    Checksum:i9EBF5FC45637645C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1544 – 15441G → A in CAA59429. (PubMed:8586427)Curated
    Sequence conflicti1544 – 15441G → A in CAA59325. 1 PublicationCurated
    Sequence conflicti1743 – 17453ATG → GMC in CAA59428. (PubMed:8586427)Curated
    Sequence conflicti1743 – 17453ATG → GMC in CAA59429. (PubMed:8586427)Curated
    Sequence conflicti2101 – 21011M → K in CAA59428. (PubMed:8586427)Curated
    Sequence conflicti2101 – 21011M → K in CAA59429. (PubMed:8586427)Curated
    Sequence conflicti2374 – 23741R → L in CAA59428. (PubMed:8586427)Curated
    Sequence conflicti2374 – 23741R → L in CAA59429. (PubMed:8586427)Curated
    Sequence conflicti2589 – 25891E → Q in CAA59428. (PubMed:8586427)Curated
    Sequence conflicti2589 – 25891E → Q in CAA59429. (PubMed:8586427)Curated
    Sequence conflicti2672 – 26721D → A in CAA59428. (PubMed:8586427)Curated
    Sequence conflicti2672 – 26721D → A in CAA59429. (PubMed:8586427)Curated
    Sequence conflicti2804 – 28041G → A in CAA59428. (PubMed:8586427)Curated
    Sequence conflicti2804 – 28041G → A in CAA59429. (PubMed:8586427)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti796 – 7961T → N.
    Corresponds to variant rs17187262 [ dbSNP | Ensembl ].
    VAR_050078
    Natural varianti1206 – 12061V → A.
    Corresponds to variant rs12457323 [ dbSNP | Ensembl ].
    VAR_050079
    Natural varianti1208 – 12081P → T.
    Corresponds to variant rs17202961 [ dbSNP | Ensembl ].
    VAR_050080
    Natural varianti1774 – 17741F → L.
    Corresponds to variant rs958631 [ dbSNP | Ensembl ].
    VAR_059444
    Natural varianti2702 – 27021T → A.
    Corresponds to variant rs9952370 [ dbSNP | Ensembl ].
    VAR_047374
    Natural varianti2815 – 28151N → K.
    Corresponds to variant rs1154232 [ dbSNP | Ensembl ].
    VAR_047375
    Natural varianti2834 – 28341S → G.3 Publications
    Corresponds to variant rs1154233 [ dbSNP | Ensembl ].
    VAR_059445

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 16201620Missing in isoform 1. 1 PublicationVSP_035738Add
    BLAST
    Alternative sequencei1 – 16091609Missing in isoform 4. 1 PublicationVSP_047079Add
    BLAST
    Alternative sequencei1610 – 166556LSRLA…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 4. 1 PublicationVSP_047080Add
    BLAST
    Alternative sequencei1621 – 166545LYFTE…AGDSC → MPPAVRRSACSMGWLWIFGA ALGQCLGYSSQQQRVPFLQP PGQSQLQASYVEFRPS in isoform 1. 1 PublicationVSP_035739Add
    BLAST
    Alternative sequencei1946 – 200257ILLKQ…ESQLL → M in isoform 3 and isoform 4. 1 PublicationVSP_043487Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY327114 mRNA. Translation: AAQ72569.1.
    AY327115 mRNA. Translation: AAQ72570.1.
    AY327116 mRNA. Translation: AAQ72571.1.
    AB107369 Genomic DNA. Translation: BAD13428.1.
    EF444992 Genomic DNA. Translation: ACA06011.1.
    AC010754 Genomic DNA. No translation available.
    AC067796 Genomic DNA. No translation available.
    AC090366 Genomic DNA. No translation available.
    X85107 mRNA. Translation: CAA59428.1.
    X85108 mRNA. Translation: CAA59429.1.
    X84900 mRNA. Translation: CAA59325.1.
    L34155 mRNA. Translation: AAA59483.1.
    CCDSiCCDS11880.1. [Q16787-1]
    CCDS42419.1. [Q16787-2]
    CCDS45838.1. [Q16787-3]
    CCDS59307.1. [Q16787-4]
    PIRiA55347.
    RefSeqiNP_000218.2. NM_000227.3.
    NP_001121189.1. NM_001127717.1. [Q16787-3]
    NP_001121190.1. NM_001127718.1. [Q16787-4]
    NP_937762.1. NM_198129.1. [Q16787-2]
    UniGeneiHs.436367.

    Genome annotation databases

    EnsembliENST00000269217; ENSP00000269217; ENSG00000053747. [Q16787-1]
    ENST00000313654; ENSP00000324532; ENSG00000053747. [Q16787-2]
    ENST00000399516; ENSP00000382432; ENSG00000053747. [Q16787-3]
    ENST00000587184; ENSP00000466557; ENSG00000053747. [Q16787-4]
    GeneIDi3909.
    KEGGihsa:3909.
    UCSCiuc002kuq.3. human. [Q16787-2]
    uc002kur.3. human. [Q16787-3]

    Polymorphism databases

    DMDMi215274012.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY327114 mRNA. Translation: AAQ72569.1 .
    AY327115 mRNA. Translation: AAQ72570.1 .
    AY327116 mRNA. Translation: AAQ72571.1 .
    AB107369 Genomic DNA. Translation: BAD13428.1 .
    EF444992 Genomic DNA. Translation: ACA06011.1 .
    AC010754 Genomic DNA. No translation available.
    AC067796 Genomic DNA. No translation available.
    AC090366 Genomic DNA. No translation available.
    X85107 mRNA. Translation: CAA59428.1 .
    X85108 mRNA. Translation: CAA59429.1 .
    X84900 mRNA. Translation: CAA59325.1 .
    L34155 mRNA. Translation: AAA59483.1 .
    CCDSi CCDS11880.1. [Q16787-1 ]
    CCDS42419.1. [Q16787-2 ]
    CCDS45838.1. [Q16787-3 ]
    CCDS59307.1. [Q16787-4 ]
    PIRi A55347.
    RefSeqi NP_000218.2. NM_000227.3.
    NP_001121189.1. NM_001127717.1. [Q16787-3 ]
    NP_001121190.1. NM_001127718.1. [Q16787-4 ]
    NP_937762.1. NM_198129.1. [Q16787-2 ]
    UniGenei Hs.436367.

    3D structure databases

    ProteinModelPortali Q16787.
    SMRi Q16787. Positions 44-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110103. 4 interactions.
    IntActi Q16787. 3 interactions.
    MINTi MINT-1431248.
    STRINGi 9606.ENSP00000324532.

    Chemistry

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

    PTM databases

    PhosphoSitei Q16787.

    Polymorphism databases

    DMDMi 215274012.

    Proteomic databases

    MaxQBi Q16787.
    PaxDbi Q16787.
    PRIDEi Q16787.

    Protocols and materials databases

    DNASUi 3909.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269217 ; ENSP00000269217 ; ENSG00000053747 . [Q16787-1 ]
    ENST00000313654 ; ENSP00000324532 ; ENSG00000053747 . [Q16787-2 ]
    ENST00000399516 ; ENSP00000382432 ; ENSG00000053747 . [Q16787-3 ]
    ENST00000587184 ; ENSP00000466557 ; ENSG00000053747 . [Q16787-4 ]
    GeneIDi 3909.
    KEGGi hsa:3909.
    UCSCi uc002kuq.3. human. [Q16787-2 ]
    uc002kur.3. human. [Q16787-3 ]

    Organism-specific databases

    CTDi 3909.
    GeneCardsi GC18P021269.
    GeneReviewsi LAMA3.
    HGNCi HGNC:6483. LAMA3.
    HPAi CAB010757.
    HPA009309.
    MIMi 226700. phenotype.
    245660. phenotype.
    600805. gene.
    neXtProti NX_Q16787.
    Orphaneti 79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
    79404. Junctional epidermolysis bullosa, Herlitz type.
    2407. LOC syndrome.
    PharmGKBi PA30272.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292643.
    HOGENOMi HOG000231235.
    HOVERGENi HBG052300.
    KOi K06240.
    OMAi RGLYFTE.
    OrthoDBi EOG7DFXB9.
    PhylomeDBi Q16787.
    TreeFami TF335359.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150268. Anchoring fibril formation.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.
    REACT_20537. Type I hemidesmosome assembly.

    Miscellaneous databases

    ChiTaRSi LAMA3. human.
    GeneWikii Laminin,_alpha_3.
    GenomeRNAii 3909.
    NextBioi 15345.
    PMAP-CutDB Q6VU68.
    PROi Q16787.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16787.
    Bgeei Q16787.
    CleanExi HS_LAMA3.
    Genevestigatori Q16787.

    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.
    [Graphical view ]
    Pfami PF00052. Laminin_B. 1 hit.
    PF00053. Laminin_EGF. 12 hits.
    PF00054. Laminin_G_1. 1 hit.
    PF02210. Laminin_G_2. 4 hits.
    PF06008. Laminin_I. 1 hit.
    PF06009. Laminin_II. 1 hit.
    PF00055. Laminin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 14 hits.
    SM00281. LamB. 1 hit.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 5 hits.
    PROSITEi PS00022. EGF_1. 12 hits.
    PS01186. EGF_2. 1 hit.
    PS01248. EGF_LAM_1. 13 hits.
    PS50027. EGF_LAM_2. 14 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    PS51115. LAMININ_IVA. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), DISEASE.
    2. "Characterization of laminin 5B and NH2-terminal proteolytic fragment of its alpha3B chain: promotion of cellular adhesion, migration, and proliferation."
      Kariya Y., Yasuda C., Nakashima Y., Ishida K., Tsubota Y., Miyazaki K.
      J. Biol. Chem. 279:24774-24784(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT GLY-2834.
    3. Stockwell T.B., Busam D.A., Ferriera S.M., Brownley A.N., Strausberg R.L., Kirkness E.F., Rogers Y.-H., Levy S.
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with Herlitz junctional epidermolysis bullosa."
      Vidal F., Baudoin C., Miquel C., Galliano M.-F., Christiano A.M., Uitto J., Ortonne J.-P., Meneguzzi G.
      Genomics 30:273-280(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2858 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1528-2858 (ISOFORMS 1/2).
      Tissue: Keratinocyte.
    6. "Mutation in LAMA3 gene in a patient affected by H-Jeb."
      Aberdam D., Vidal F., Baudoin C., Miquel C., Ortonne J.-P., Meneguzzi G.
      Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1528-3333 (ISOFORMS 1/2), VARIANT GLY-2834.
    7. "Cloning of the LamA3 gene encoding the alpha 3 chain of the adhesive ligand epiligrin. Expression in wound repair."
      Ryan M.C., Tizard R., Vandevanter D.R., Carter W.G.
      J. Biol. Chem. 269:22779-22787(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-2834.
      Tissue: Keratinocyte.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLAMA3_HUMAN
    AccessioniPrimary (citable) accession number: Q16787
    Secondary accession number(s): B0YJ33
    , Q13679, Q13680, Q6VU67, Q6VU68, Q6VU69, Q76E14, Q96TG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 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 18
      Human chromosome 18: 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