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Q61789

- LAMA3_MOUSE

UniProt

Q61789 - LAMA3_MOUSE

Protein

Laminin subunit alpha-3

Gene

Lama3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 4 (16 Oct 2013)
      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.By similarity

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. regulation of cell adhesion Source: InterPro
    3. regulation of cell migration Source: InterPro
    4. regulation of embryonic development Source: InterPro

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_196595. Anchoring fibril formation.
    REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_202342. Laminin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit alpha-3
    Alternative name(s):
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:99909. Lama3.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 31311 PublicationAdd
    BLAST
    Chaini32 – 33303299Laminin subunit alpha-3PRO_0000017059Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi296 ↔ 305By similarity
    Disulfide bondi298 ↔ 316By similarity
    Disulfide bondi318 ↔ 327By similarity
    Disulfide bondi330 ↔ 350By similarity
    Disulfide bondi353 ↔ 362By similarity
    Disulfide bondi355 ↔ 387By similarity
    Disulfide bondi390 ↔ 399By similarity
    Disulfide bondi402 ↔ 420By similarity
    Disulfide bondi423 ↔ 433By similarity
    Disulfide bondi425 ↔ 440By similarity
    Disulfide bondi442 ↔ 451By similarity
    Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi454 ↔ 464By similarity
    Disulfide bondi488 ↔ 500By similarity
    Disulfide bondi490 ↔ 506By similarity
    Disulfide bondi508 ↔ 517By similarity
    Disulfide bondi520 ↔ 530By similarity
    Disulfide bondi533 ↔ 545By similarity
    Disulfide bondi535 ↔ 552By similarity
    Disulfide bondi554 ↔ 563By similarity
    Disulfide bondi566 ↔ 583By similarity
    Disulfide bondi628 ↔ 642By similarity
    Disulfide bondi630 ↔ 649By similarity
    Disulfide bondi651 ↔ 660By similarity
    Disulfide bondi663 ↔ 678By similarity
    Disulfide bondi681 ↔ 693By similarity
    Disulfide bondi683 ↔ 700By similarity
    Disulfide bondi702 ↔ 711By similarity
    Disulfide bondi1309 ↔ 1316By similarity
    Disulfide bondi1311 ↔ 1323By similarity
    Disulfide bondi1325 ↔ 1334By similarity
    Disulfide bondi1337 ↔ 1350By similarity
    Disulfide bondi1353 ↔ 1368By similarity
    Glycosylationi1354 – 13541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1355 ↔ 1375By similarity
    Disulfide bondi1377 ↔ 1386By similarity
    Disulfide bondi1389 ↔ 1399By similarity
    Disulfide bondi1402 ↔ 1414By similarity
    Disulfide bondi1404 ↔ 1421By similarity
    Disulfide bondi1423 ↔ 1432By similarity
    Disulfide bondi1435 ↔ 1450By similarity
    Glycosylationi1673 – 16731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1684 ↔ 1693By similarity
    Disulfide bondi1686 ↔ 1700By similarity
    Disulfide bondi1703 ↔ 1712By similarity
    Disulfide bondi1715 ↔ 1728By similarity
    Disulfide bondi1731 ↔ 1743By similarity
    Disulfide bondi1733 ↔ 1752By similarity
    Disulfide bondi1754 ↔ 1763By similarity
    Disulfide bondi1766 ↔ 1781By similarity
    Disulfide bondi1819 – 1819InterchainCurated
    Disulfide bondi1822 – 1822InterchainCurated
    Glycosylationi2159 – 21591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2261 – 22611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2332 – 23321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2361 – 23611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2498 – 24981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2557 ↔ 2587By similarity
    Glycosylationi2580 – 25801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2733 ↔ 2756By similarity
    Glycosylationi2747 – 27471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2891 ↔ 2923By similarity
    Glycosylationi3094 – 30941N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3124 ↔ 3147By similarity
    Glycosylationi3270 – 32701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3299 ↔ 3327By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ61789.
    PaxDbiQ61789.
    PRIDEiQ61789.

    PTM databases

    PhosphoSiteiQ61789.

    Expressioni

    Tissue specificityi

    Basal membrane of the upper alimentary tract and urinary and nasal epithelia, salivary glands and teeth (both variants). Isoform A is predominantly expressed in skin, hair follicles and developing neurons of the trigeminal ganglion. Isoform B was found in bronchi, alveoli, stomach, intestinal crypts, whisker pads, CNS, telencephalic neuroectoderm, thalamus, Rathke pouch and periventricular subependymal germinal layer.

    Gene expression databases

    BgeeiE9PUR4.
    CleanExiMM_LAMA3.
    GenevestigatoriQ61789.

    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).

    Structurei

    3D structure databases

    ProteinModelPortaliQ61789.
    SMRiQ61789. Positions 43-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 295256Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini296 – 35055Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini353 – 42068Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini423 – 46442Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini488 – 53043Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini533 – 57644Laminin EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini582 – 62544Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini628 – 67851Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini681 – 72545Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1309 – 135244Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1353 – 140149Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1402 – 145251Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1453 – 146210Laminin EGF-like 12; first partPROSITE-ProRule annotation
    Domaini1466 – 1650185Laminin IV type APROSITE-ProRule annotationAdd
    BLAST
    Domaini1651 – 168333Laminin EGF-like 12; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1684 – 173047Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1731 – 178353Laminin EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1784 – 181835Laminin EGF-like 15; truncatedPROSITE-ProRule annotationAdd
    BLAST
    Domaini2386 – 2587202Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2594 – 2756163Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2763 – 2923161Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini2983 – 3147165Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini3154 – 3327174Laminin G-like 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni295 – 725431Domain VAdd
    BLAST
    Regioni793 – 1262470Domain IV 1 (domain IV B)Add
    BLAST
    Regioni1263 – 1462200Domain III BAdd
    BLAST
    Regioni1651 – 1818168Domain III AAdd
    BLAST
    Regioni1819 – 2385567Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1851 – 1980130Sequence AnalysisAdd
    BLAST
    Coiled coili2012 – 205746Sequence AnalysisAdd
    BLAST
    Coiled coili2088 – 216578Sequence AnalysisAdd
    BLAST
    Coiled coili2211 – 223828Sequence AnalysisAdd
    BLAST
    Coiled coili2318 – 238366Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2274 – 22763Cell 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.
    Domains IV and G are 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.
    GeneTreeiENSGT00750000117549.
    HOGENOMiHOG000048708.
    HOVERGENiHBG052300.
    KOiK06240.
    OMAiRGLYFTE.
    OrthoDBiEOG7DFXB9.
    TreeFamiTF335359.

    Family and domain databases

    Gene3Di2.60.120.200. 5 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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. 13 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. 13 hits.
    SM00281. LamB. 1 hit.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 5 hits.
    PROSITEiPS00022. EGF_1. 11 hits.
    PS01186. EGF_2. 1 hit.
    PS01248. EGF_LAM_1. 12 hits.
    PS50027. EGF_LAM_2. 13 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    PS51115. LAMININ_IVA. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: Q61789-1) [UniParc]FASTAAdd to Basket

    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

    MAVALGRAPR SLPLLLTLLL LLLLRMSPSW SVVGQDHPMS SRSLHPPYFN     50
    LAQAARIWAT ATCGERDPEV SRPRPELFCK LVGGPAAQGS GHTIQGQFCD 100
    YCNSEDSRKA HPASHAIDGS ERWWQSPPLS SGTQYNQVNL TLDLGQLFHV 150
    AYILIKFANS PRPDLWILER SVDFGSTYSP WQYFAHSRRD CVEQFGQEAN 200
    MAITQDDQML CVTEYSRIVP LENGEIVVSL INGRPGAKKF AFSDTLREFT 250
    KATNIRLRFL RTNTLLGHLI SKAERDPTVT RRYYYSIKDI SVGGRCVCNG 300
    HAEACSADNP EKQFRCECQH HTCGDTCNRC CAGYNQRRWQ PAGQEQHNEC 350
    EACNCHGHAV DCYYDPDVEH QQASLNSKGV YAGGGVCINC QHNTAGVNCE 400
    KCAKGYFRPH GVPVDALHGC IPCSCDPERA DDCDQGSGHC HCKPNFSGDY 450
    CETCADGYYN FPFCLRIPVF PNYTPSPEDP VAGNIKGCDC NLEGVLPEIC 500
    DDRGRCLCRP GVEGPQCDSC RSGSYSFPIC QACQCSTIGS YPVPCDPGNG 550
    QCDCLPGITG RQCDRCLSGA YDFPYCQGSG SVCHPAGTLD SSLGYCQCKQ 600
    HVASPTCSVC KPLYWNLAKE NPRGCSECQC HEAGTLSGIG ECGQEDGDCS 650
    CKAHVTGDAC DTCEDGFFSL EKSNYFGCQG CQCDIGGALT TMCSGPSGVC 700
    QCREHVEGKQ CQRPENNYYF PDLHHMKYEV EDGTGPNGRN LRFGFDPLVF 750
    PEFSWRGYAP MTSVQNEVRV RLSVRQSSLS LFRIVLRYIS PGTEAISGRI 800
    TLYSSQGDSD ALQSRKITFP PSKEPAFVTV PGNGFAGPFS ITPGTWIACI 850
    QVEGVLLDYL VLLPRDYYEA FTLQVPVTEP CAHTGSPQDN CLLYQHLPLT 900
    AFSCTLACEA RHFLLDGELR PLAMRQPTPT HPAMVDLSGR EVELQLRLRV 950
    PQVGHYVVLL EYATEVEQLF VVDVNLKSSG SALAGQVNIY SCKYSIPCRS 1000
    VVIDSLSRTA VHELLADADI QLKAHMAHFL LYHICIIPAE EFSTEYLRPQ 1050
    VHCIASYRQH ANPSASCVSL AHETPPTASI LDATSRGLFS ALPHEPSSPA 1100
    DGVTLKAPQS QVTLKGLIPH LGRHVFVIHF YQAEHPGFPT EVIVNGGRQW 1150
    SGSFLASFCP HLLGCRDQVI SDGQVEFDIS EAEVAVTVKI PDGKSLTLVR 1200
    VLVVPAENYD YQILHKTTVD KSSEFISSCG GDSFYIDPQA ASGFCKNSAR 1250
    SLVAFYHNGA IPCECDPAGT AGHHCSPEGG QCPCRPNVIG RQCSRCATGY 1300
    YGFPYCKPCN CGRRLCEEVT GKCLCPPHTV RPQCEVCEMN SFNFHPVAGC 1350
    DVCNCSRKGT IEAAVSECDR DSGQCRCKPR VTGQQCDKCA PGFYQFPECV 1400
    PCSCNRDGTE PSVCDPETGA CMCKENVEGP QCQLCREGSF YLDPTNPKGC 1450
    TKCFCFGVNT DCQSSHKQRA KFVDMMGWRL ETADGVDVPV SFNPGSNSMV 1500
    ADLQELPPSV HSASWVAPPS YLGDKVSSYG GYLTYHAKSF GLPGDMVLLG 1550
    KQPDVQLTGQ HMSLIHKEPS DPRPDRLHHG RVQVIEGNFR HEGSSAPVSR 1600
    EELMTVLSRL ERLHIRGLHF TETQRLTLGE VGLEEASDTG SGPRAHLVEM 1650
    CACPPDYTGD SCQGCRPGYY WDNKSLPVGR CVPCNCNGHS NRCQDGSGIC 1700
    INCQHNTAGE HCERCQAGHY GNAIHGSCRV CPCPHTNSFA TGCAVDGGAV 1750
    RCACKPGYTG TQCERCAPGY FGNPQKFGGS CQPCNCNSNG QLGPCDPLTG 1800
    DCVNQEPKDG SPAEECDDCD SCVMTLLNDL ASMGEELRLV KSKLQGLSVS 1850
    TGALEQIRHM ETQAKDLRNQ LLGFRSATSS HGSKMDDLEK ELSHLNREFE 1900
    TLQEKAQVNS RKAQTLYNNI DQTIQSAKEL DMKIKNIVQN VHILLKQMAR 1950
    PGGEGTDLPV GDWSRELAEA QRMMRDLRSR DFKKHLQEAE AEKMEAQLLL 2000
    HRIRTWLESH QVENNGLLKN IRDSLNDYED KLQDLRSILQ EAAAQAKQAT 2050
    GINHENEGVL GAIQRQMKEM DSLKNDFTKY LATADSSLLQ TNNLLQQMDK 2100
    SQKEYESLAA ALNGARQELS DRVRELSRSG GKAPLVVEAE KHAQSLQELA 2150
    KQLEEIKRNT SGDELVRCAV DAATAYENIL NAIRAAEDAA SKATSASKSA 2200
    FQTVIKEDLP KRAKTLSSDS EELLNEAKMT QKRLQQVSPA LNSLQQTLKT 2250
    VSVQKDLLDA NLTVARDDLH GIQRGDIDSV VIGAKSMVRE ANGITSEVLD 2300
    GLNPIQTDLG RIKDSYESAR REDFSKALVD ANNSVKKLTR KLPDLFIKIE 2350
    SINQQLLPLG NISDNVDRIR ELIQQARDAA NKVAIPMRFN GKSGVEVRLP 2400
    NDLEDLKGYT SLSLFLQRPD LRENGGTEDM FVMYLGNKDA SKDYIGMAVV 2450
    DGQLTCVYNL GDREAEVQID QVLTESESQE AVMDRVKFQR IYQFAKLNYT 2500
    KEATSTKPKA PGVYDMESAS SNTLLNLDPE NAVFYVGGYP PGFELPRRLR 2550
    FPPYKGCIEL DDLNENVLSL YNFKTTFNLN TTEVEPCRRR KEESDKNYFE 2600
    GTGYARIPTQ PNAPFPNFMQ TIQTTVDRGL LFFAENQDNF ISLNIEDGNL 2650
    MVKYKLNSEP PKEKGIRDTI NNGRDHMILI SIGKSQKRML INMNKHSIII 2700
    EGEIFDFSTY YLGGIPIAIR ERFNISTPAF QGCMKNLKKT SGVVRLNDTV 2750
    GVTKKCSEDW KLVRTASFSR GGQMSFTNLD VPSLDRFQLS FGFQTFQPSG 2800
    TLLNHQTRTS SLLVTLEDGH IALSTRDSSS PIFKSPGTYM DGLLHHVSVI 2850
    SDTSGLRLLI DDQVLRRNQR LASFSNAQQS LSMGGGYFEG CISNVFVQRM 2900
    SQSPEVLDMA SKSTKRDAFL GGCSLNKPPF LMLFKSPKGF NKARSFNVNQ 2950
    LLQDAPQAAR SIEAWQDGKS CLPPLNTKAT HRALQFGDSP TSHLLFKLPQ 3000
    ELLKPRLQFS LDIQTTSSRG LVFHTGTRDS FVALYLSEGH VIFALGAGGK 3050
    KLRLRSKERY HDGKWHSVVF GLSGRKVHLV VDGLRAQEGS LPGNSTISPR 3100
    EQVYLGLSPS RKSKSLPQHS FVGCLRNFQL DSKPLDSPSA RSGVSPCLGG 3150
    SLEKGIYFSQ GGGHVVLANS VSLEPALTLT LSIRPRSLTG VLIHIASQSG 3200
    EHLSVYMEAG KVTTSMNSEA GGTVTSITPK RSLCDGQWHS VTVSIKQHTL 3250
    HLELDTDNSY TAGQLSFPPN STRGSLHIGG VPDKLKMLTL PVWNSFFGCL 3300
    KNIQVNHIPV PITEATDVQG SVSLNGCPDH 3330
    Length:3,330
    Mass (Da):366,227
    Last modified:October 16, 2013 - v4
    Checksum:i993EB20BACDD6C59
    GO
    Isoform A (identifier: Q61789-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1619: Missing.
         1620-1662: FTETQRLTLG...CPPDYTGDSC → MLPAVRWSAW...QASYMELRPS

    Show »
    Length:1,724
    Mass (Da):190,610
    Checksum:i01153704F6DC87C3
    GO

    Sequence cautioni

    The sequence CAA58837.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti982 – 9821A → R in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1150 – 11501W → R in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1224 – 12241E → K in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1272 – 12721G → GH in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1291 – 12911R → S in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1398 – 13981E → K in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1466 – 14661H → R in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1479 – 14791R → V in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1488 – 14881V → F in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1527 – 15282SS → II in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1608 – 16081S → P in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1983 – 19842KK → QN in CAA58836. (PubMed:7665604)Curated
    Sequence conflicti1983 – 19842KK → QN in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1983 – 19842KK → QN in AAA68091. (PubMed:8012114)Curated
    Sequence conflicti1987 – 19871Q → G in CAA58836. (PubMed:7665604)Curated
    Sequence conflicti1987 – 19871Q → G in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti1987 – 19871Q → G in AAA68091. (PubMed:8012114)Curated
    Sequence conflicti2463 – 24631R → G in CAA58836. (PubMed:7665604)Curated
    Sequence conflicti2463 – 24631R → G in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti2463 – 24631R → G in AAA68091. (PubMed:8012114)Curated
    Sequence conflicti2488 – 24881F → S in CAA58836. (PubMed:7665604)Curated
    Sequence conflicti2488 – 24881F → S in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti2488 – 24881F → S in AAA68091. (PubMed:8012114)Curated
    Sequence conflicti2617 – 26204NFMQ → KLSW in CAA58836. (PubMed:7665604)Curated
    Sequence conflicti2617 – 26204NFMQ → KLSW in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti2724 – 27252NI → PL in CAA58836. (PubMed:7665604)Curated
    Sequence conflicti2724 – 27252NI → PL in CAA58837. (PubMed:7665604)Curated
    Sequence conflicti3257 – 32571D → Y in CAA58836. (PubMed:7665604)Curated
    Sequence conflicti3257 – 32571D → Y in CAA58837. (PubMed:7665604)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 16191619Missing in isoform A. 1 PublicationVSP_003038Add
    BLAST
    Alternative sequencei1620 – 166243FTETQ…TGDSC → MLPAVRWSAWSTGWLWIFGA ALGQCLGYGSEQQRVAFLQR PSQNHLQASYMELRPS in isoform A. 1 PublicationVSP_003039Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84013 mRNA. Translation: CAA58836.1.
    X84014 mRNA. Translation: CAA58837.1. Frameshift.
    AC102131 Genomic DNA. No translation available.
    AC102248 Genomic DNA. No translation available.
    AC139027 Genomic DNA. No translation available.
    AC157909 Genomic DNA. No translation available.
    AJ293592 mRNA. Translation: CAB99254.2.
    U88353 mRNA. Translation: AAC53179.1.
    L20478 mRNA. Translation: AAA68091.1.
    CCDSiCCDS50222.1. [Q61789-1]
    RefSeqiNP_034810.1. NM_010680.1. [Q61789-1]
    XP_006525753.1. XM_006525690.1. [Q61789-2]
    UniGeneiMm.42012.

    Genome annotation databases

    EnsembliENSMUST00000092070; ENSMUSP00000089703; ENSMUSG00000024421. [Q61789-1]
    GeneIDi16774.
    KEGGimmu:16774.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X84013 mRNA. Translation: CAA58836.1 .
    X84014 mRNA. Translation: CAA58837.1 . Frameshift.
    AC102131 Genomic DNA. No translation available.
    AC102248 Genomic DNA. No translation available.
    AC139027 Genomic DNA. No translation available.
    AC157909 Genomic DNA. No translation available.
    AJ293592 mRNA. Translation: CAB99254.2 .
    U88353 mRNA. Translation: AAC53179.1 .
    L20478 mRNA. Translation: AAA68091.1 .
    CCDSi CCDS50222.1. [Q61789-1 ]
    RefSeqi NP_034810.1. NM_010680.1. [Q61789-1 ]
    XP_006525753.1. XM_006525690.1. [Q61789-2 ]
    UniGenei Mm.42012.

    3D structure databases

    ProteinModelPortali Q61789.
    SMRi Q61789. Positions 43-424.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q61789.

    Proteomic databases

    MaxQBi Q61789.
    PaxDbi Q61789.
    PRIDEi Q61789.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000092070 ; ENSMUSP00000089703 ; ENSMUSG00000024421 . [Q61789-1 ]
    GeneIDi 16774.
    KEGGi mmu:16774.

    Organism-specific databases

    CTDi 3909.
    MGIi MGI:99909. Lama3.

    Phylogenomic databases

    eggNOGi NOG292643.
    GeneTreei ENSGT00750000117549.
    HOGENOMi HOG000048708.
    HOVERGENi HBG052300.
    KOi K06240.
    OMAi RGLYFTE.
    OrthoDBi EOG7DFXB9.
    TreeFami TF335359.

    Enzyme and pathway databases

    Reactomei REACT_196595. Anchoring fibril formation.
    REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_202342. Laminin interactions.

    Miscellaneous databases

    NextBioi 290610.
    PROi Q61789.
    SOURCEi Search...

    Gene expression databases

    Bgeei E9PUR4.
    CleanExi MM_LAMA3.
    Genevestigatori Q61789.

    Family and domain databases

    Gene3Di 2.60.120.200. 5 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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. 13 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. 13 hits.
    SM00281. LamB. 1 hit.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 5 hits.
    PROSITEi PS00022. EGF_1. 11 hits.
    PS01186. EGF_2. 1 hit.
    PS01248. EGF_LAM_1. 12 hits.
    PS50027. EGF_LAM_2. 13 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    PS51115. LAMININ_IVA. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and complete primary structure of the mouse laminin alpha 3 chain. Distinct expression pattern of the laminin alpha 3A and alpha 3B chain isoforms."
      Galliano M.-F., Aberdam D., Aguzzi A., Ortonne J.-P., Meneguzzi G.
      J. Biol. Chem. 270:21820-21826(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), NUCLEOTIDE SEQUENCE [MRNA] OF 765-3330 (ISOFORM B).
      Strain: BALB/c.
      Tissue: Lung.
    2. Aberdam D.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "Complete sequence, recombinant analysis and binding to laminins and sulphated ligands of the N-terminal domains of laminin alpha3B and alpha5 chains."
      Garbe J.H., Gohring W., Mann K., Timpl R., Sasaki T.
      Biochem. J. 362:213-221(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-58 (ISOFORM B), PROTEIN SEQUENCE OF 32-38.
    5. "The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform."
      Miner J.H., Patton B.L., Lentz S.I., Gilbert D.J., Snider W.D., Jenkins N.A., Copeland N.G., Sanes J.R.
      J. Cell Biol. 137:685-701(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-776 (ISOFORM B).
      Strain: ICR.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1813-2531 (ISOFORM B).
      Tissue: Lung.

    Entry informationi

    Entry nameiLAMA3_MOUSE
    AccessioniPrimary (citable) accession number: Q61789
    Secondary accession number(s): E9PUR4
    , O08751, Q61788, Q61966, Q9JHQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: October 16, 2013
    Last modified: October 1, 2014
    This is version 137 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3