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P19137

- LAMA1_MOUSE

UniProt

P19137 - LAMA1_MOUSE

Protein

Laminin subunit alpha-1

Gene

Lama1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      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. extracellular matrix structural constituent Source: MGI
    2. glycosphingolipid binding Source: MGI
    3. protein binding Source: IntAct

    GO - Biological processi

    1. branching involved in salivary gland morphogenesis Source: MGI
    2. cell adhesion Source: UniProtKB-KW
    3. cell surface receptor signaling pathway Source: MGI
    4. epithelial tube branching involved in lung morphogenesis Source: MGI
    5. establishment of epithelial cell apical/basal polarity Source: MGI
    6. morphogenesis of an epithelial sheet Source: MGI
    7. neuron projection development Source: MGI
    8. regulation of cell adhesion Source: InterPro
    9. regulation of cell migration Source: InterPro
    10. regulation of embryonic development Source: InterPro
    11. retina development in camera-type eye Source: MGI
    12. retinal blood vessel morphogenesis Source: MGI
    13. tissue development Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_202342. Laminin interactions.
    REACT_219680. L1CAM interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit alpha-1
    Alternative name(s):
    Laminin A chain
    Laminin-1 subunit alpha
    Laminin-3 subunit alpha
    S-laminin subunit alpha
    Short name:
    S-LAM alpha
    Gene namesi
    Name:Lama1
    Synonyms:Lama, Lama-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:99892. Lama1.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: MGI
    2. basement membrane Source: UniProtKB
    3. cell-cell junction Source: MGI
    4. extracellular matrix Source: MGI
    5. extracellular region Source: Reactome
    6. laminin-1 complex Source: MGI
    7. laminin complex Source: MGI
    8. proteinaceous extracellular matrix Source: MGI

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 30843060Laminin subunit alpha-1PRO_0000017055Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Pyrrolidone carboxylic acid1 Publication
    Glycosylationi45 – 451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi277 ↔ 286By similarity
    Disulfide bondi279 ↔ 297By similarity
    Disulfide bondi299 ↔ 308By similarity
    Disulfide bondi311 ↔ 331By similarity
    Disulfide bondi334 ↔ 343By similarity
    Disulfide bondi336 ↔ 368By similarity
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi371 ↔ 380By similarity
    Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi383 ↔ 401By similarity
    Disulfide bondi404 ↔ 416By similarity
    Disulfide bondi406 ↔ 434By similarity
    Disulfide bondi436 ↔ 445By similarity
    Disulfide bondi448 ↔ 458By similarity
    Disulfide bondi461 ↔ 474By similarity
    Disulfide bondi463 ↔ 478By similarity
    Disulfide bondi480 ↔ 489By similarity
    Disulfide bondi492 ↔ 507By similarity
    Glycosylationi531 – 5311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi562 – 5621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi672 – 6721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi749 ↔ 758By similarity
    Disulfide bondi751 ↔ 764By similarity
    Disulfide bondi767 ↔ 776By similarity
    Glycosylationi770 – 7701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi779 ↔ 795By similarity
    Disulfide bondi798 ↔ 813By similarity
    Disulfide bondi800 ↔ 823By similarity
    Disulfide bondi826 ↔ 835By similarity
    Disulfide bondi838 ↔ 853By similarity
    Disulfide bondi856 ↔ 870By similarity
    Glycosylationi857 – 8571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi858 ↔ 877By similarity
    Disulfide bondi880 ↔ 889By similarity
    Disulfide bondi892 ↔ 906By similarity
    Disulfide bondi909 ↔ 921By similarity
    Disulfide bondi911 ↔ 928By similarity
    Glycosylationi914 – 9141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi930 ↔ 939By similarity
    Disulfide bondi942 ↔ 955By similarity
    Disulfide bondi958 ↔ 970By similarity
    Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi960 ↔ 976By similarity
    Glycosylationi969 – 9691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi978 ↔ 987By similarity
    Disulfide bondi990 ↔ 1002By similarity
    Disulfide bondi1005 ↔ 1014By similarity
    Disulfide bondi1007 ↔ 1021By similarity
    Disulfide bondi1023 ↔ 1032By similarity
    Disulfide bondi1035 ↔ 1048By similarity
    Disulfide bondi1051 ↔ 1063By similarity
    Glycosylationi1052 – 10521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1053 ↔ 1070By similarity
    Disulfide bondi1072 ↔ 1081By similarity
    Disulfide bondi1084 ↔ 1094By similarity
    Disulfide bondi1097 ↔ 1109By similarity
    Disulfide bondi1099 ↔ 1125By similarity
    Disulfide bondi1127 ↔ 1136By similarity
    Disulfide bondi1139 ↔ 1154By similarity
    Glycosylationi1344 – 13441N-linked (GlcNAc...)1 Publication
    Disulfide bondi1410 ↔ 1419By similarity
    Disulfide bondi1412 ↔ 1426By similarity
    Glycosylationi1414 – 14141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1429 ↔ 1438By similarity
    Disulfide bondi1441 ↔ 1456By similarity
    Disulfide bondi1459 ↔ 1473By similarity
    Disulfide bondi1461 ↔ 1483By similarity
    Disulfide bondi1486 ↔ 1495By similarity
    Disulfide bondi1498 ↔ 1513By similarity
    Disulfide bondi1516 ↔ 1528By similarity
    Disulfide bondi1518 ↔ 1535By similarity
    Disulfide bondi1537 ↔ 1546By similarity
    Disulfide bondi1549 ↔ 1560By similarity
    Disulfide bondi1563 – 1563InterchainCurated
    Disulfide bondi1567 – 1567InterchainCurated
    Glycosylationi1586 – 15861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1603 – 16031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1659 – 16591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1686 – 16861N-linked (GlcNAc...)1 Publication
    Glycosylationi1706 – 17061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1718 – 17181N-linked (GlcNAc...)1 Publication
    Glycosylationi1725 – 17251N-linked (GlcNAc...)1 Publication
    Glycosylationi1763 – 17631N-linked (GlcNAc...)1 Publication
    Glycosylationi1812 – 18121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1902 – 19021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1906 – 19061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1936 – 19361N-linked (GlcNAc...)1 Publication
    Glycosylationi1982 – 19821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1993 – 19931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1999 – 19991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2027 – 20271N-linked (GlcNAc...)1 Publication
    Glycosylationi2046 – 20461N-linked (GlcNAc...)1 Publication
    Glycosylationi2055 – 20551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2062 – 20621N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi2067 – 20671N-linked (GlcNAc...)1 Publication
    Glycosylationi2102 – 21021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2106 – 21061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2251 – 22511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2252 – 22521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2279 ↔ 2305By similarity
    Glycosylationi2356 – 23561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2392 – 23921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2465 ↔ 2489By similarity
    Glycosylationi2526 – 25261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2653 ↔ 2680By similarity
    Glycosylationi2738 – 27381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2835 – 28351N-linked (GlcNAc...)1 Publication
    Disulfide bondi2869 ↔ 2894By similarity
    Glycosylationi2924 – 29241N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3048 ↔ 3079By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP19137.
    PaxDbiP19137.
    PRIDEiP19137.

    PTM databases

    PhosphoSiteiP19137.

    Expressioni

    Gene expression databases

    CleanExiMM_LAMA1.
    GenevestigatoriP19137.

    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-1 is a subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3 (laminin-121 or S-laminin).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAG1O187382EBI-7176628,EBI-8522926From a different organism.

    Protein-protein interaction databases

    BioGridi201096. 7 interactions.
    IntActiP19137. 4 interactions.
    MINTiMINT-2635122.
    STRINGi10090.ENSMUSP00000043957.

    Structurei

    Secondary structure

    1
    3084
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2732 – 27365
    Beta strandi2743 – 275412
    Beta strandi2759 – 27657
    Beta strandi2769 – 277810
    Beta strandi2781 – 27877
    Beta strandi2792 – 27965
    Beta strandi2803 – 28053
    Beta strandi2807 – 28148
    Beta strandi2817 – 28226
    Beta strandi2843 – 28497
    Beta strandi2868 – 28758
    Beta strandi2886 – 28905
    Beta strandi2895 – 291723
    Beta strandi2923 – 293210
    Beta strandi2936 – 29427
    Beta strandi2944 – 29463
    Beta strandi2948 – 29547
    Beta strandi2957 – 296610
    Beta strandi2968 – 29736
    Helixi2980 – 29823
    Beta strandi2983 – 29853
    Beta strandi2987 – 29948
    Beta strandi2997 – 30026
    Beta strandi3005 – 30095
    Beta strandi3023 – 30286
    Beta strandi3046 – 30549
    Helixi3065 – 30673
    Beta strandi3069 – 30757
    Beta strandi3079 – 30813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JD4X-ray1.90A/B2706-3084[»]
    ProteinModelPortaliP19137.
    SMRiP19137. Positions 29-523, 715-1154, 1369-1558, 2140-3083.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19137.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 276252Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini277 – 33357Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini334 – 40370Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini404 – 46057Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini461 – 50949Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini510 – 51910Laminin EGF-like 5; first partPROSITE-ProRule annotation
    Domaini523 – 715193Laminin IV type A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini716 – 74833Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini749 – 79749Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini798 – 85558Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini856 – 90853Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini909 – 95749Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini958 – 100447Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1005 – 105046Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1051 – 109646Laminin EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1097 – 115660Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1157 – 116610Laminin EGF-like 14; first partPROSITE-ProRule annotation
    Domaini1177 – 1368192Laminin IV type A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1369 – 140941Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1410 – 145849Laminin EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1459 – 151557Laminin EGF-like 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini1516 – 156247Laminin EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2125 – 2305181Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2313 – 2489177Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2494 – 2680187Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini2722 – 2894173Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2899 – 3079181Laminin G-like 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1564 – 2124561Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1612 – 1820209Sequence AnalysisAdd
    BLAST
    Coiled coili1869 – 190335Sequence AnalysisAdd
    BLAST
    Coiled coili2096 – 212833Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1147 – 11493Cell attachment site

    Domaini

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

    Sequence similaritiesi

    Contains 17 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 5 laminin G-like domains.PROSITE-ProRule annotation
    Contains 2 laminin IV type A domains.PROSITE-ProRule annotation
    Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Laminin EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG247347.
    HOGENOMiHOG000293201.
    HOVERGENiHBG052298.
    InParanoidiP19137.
    KOiK05637.
    PhylomeDBiP19137.

    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. 2 hits.
    PF00053. Laminin_EGF. 17 hits.
    PF00054. Laminin_G_1. 4 hits.
    PF02210. Laminin_G_2. 1 hit.
    PF06008. Laminin_I. 1 hit.
    PF06009. Laminin_II. 1 hit.
    PF00055. Laminin_N. 1 hit.
    [Graphical view]
    SMARTiSM00180. EGF_Lam. 15 hits.
    SM00281. LamB. 2 hits.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 5 hits.
    PROSITEiPS00022. EGF_1. 11 hits.
    PS01186. EGF_2. 3 hits.
    PS01248. EGF_LAM_1. 15 hits.
    PS50027. EGF_LAM_2. 15 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    PS51115. LAMININ_IVA. 2 hits.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P19137-1 [UniParc]FASTAAdd to Basket

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    MRGSGTGAAL LVLLASVLWV TVRSQQRGLF PAILNLATNA HISANATCGE     50
    KGPEMFCKLV EHVPGRPVRH AQCRVCDGNS TNPRERHPIS HAIDGTNNWW 100
    QSPSIQNGRE YHWVTVTLDL RQVFQVAYII IKAANAPRPG NWILERSVDG 150
    VKFKPWQYYA VSDTECLTRY KITPRRGPPT YRADNEVICT SYYSKLVPLE 200
    HGEIHTSLIN GRPSADDPSP QLLEFTSARY IRLRLQRIRT LNADLMTLSH 250
    RDLRDLDPIV TRRYYYSIKD ISVGGMCICY GHASSCPWDE EAKQLQCQCE 300
    HNTCGESCDR CCPGYHQQPW RPGTISSGNE CEECNCHNKA KDCYYDSSVA 350
    KERRSLNTAG QYSGGGVCVN CSQNTTGINC ETCIDQYYRP HKVSPYDDHP 400
    CRPCNCDPVG SLSSVCIKDD RHADLANGKW PGQCPCRKGY AGDKCDRCQF 450
    GYRGFPNCIP CDCRTVGSLN EDPCIEPCLC KKNVEGKNCD RCKPGFYNLK 500
    ERNPEGCSEC FCFGVSGVCD SLTWSISQVT NMSGWLVTDL MSTNKIRSQQ 550
    DVLGGHRQIS INNTAVMQRL TSTYYWAAPE AYLGNKLTAF GGFLKYTVSY 600
    DIPVETVDSD LMSHADIIIK GNGLTISTRA EGLSLQPYEE YFNVVRLVPE 650
    NFRDFNTRRE IDRDQLMTVL ANVTHLLIRA NYNSAKMALY RLDSVSLDIA 700
    SPNAIDLAVA ADVEHCECPQ GYTGTSCEAC LPGYYRVDGI LFGGICQPCE 750
    CHGHASECDI HGICSVCTHN TTGDHCEQCL PGFYGTPSRG TPGDCQPCAC 800
    PLSIDSNNFS PTCHLTDGEE VVCDQCAPGY SGSWCERCAD GYYGNPTVPG 850
    GTCVPCNCSG NVDPLEAGHC DSVTGECLKC LWNTDGAHCE RCADGFYGDA 900
    VTAKNCRACD CHENGSLSGV CHLETGLCDC KPHVTGQQCD QCLSGYYGLD 950
    TGLGCVPCNC SVEGSVSDNC TEEGQCHCGP GVSGKQCDRC SHGFYAFQDG 1000
    GCTPCDCAHT QNNCDPASGE CLCPPHTQGL KCEECEEAYW GLDPEQGCQA 1050
    CNCSAVGSTS AQCDVLSGHC PCKKGFGGQS CHQCSLGYRS FPDCVPCGCD 1100
    LRGTLPDTCD LEQGLCSCSE DSGTCSCKEN VVGPQCSKCQ AGTFALRGDN 1150
    PQGCSPCFCF GLSQLCSELE GYVRTLITLA SDQPLLHVVS QSNLKGTIEG 1200
    VHFQPPDTLL DAEAVRQHIY AEPFYWRLPK QFQGDQLLAY GGKLQYSVAF 1250
    YSTLGTGTSN YEPQVLIKGG RARKHVIYMD APAPENGVRQ DYEVQMKEEF 1300
    WKYFNSVSEK HVTHSDFMSV LSNIDYILIK ASYGQGLQQS RIANISMEVG 1350
    RKAVELPAEG EAALLLELCV CPPGTAGHSC QDCAPGYYRE KLPESGGRGP 1400
    RPLLAPCVPC NCNNHSDVCD PETGKCLSCR DHTSGDHCEL CASGYYGKVT 1450
    GLPGDCTPCT CPHHPPFSFS PTCVVEGDSD FRCNACLPGY EGQYCERCSA 1500
    GYHGNPRAAG GSCQTCDCNP QGSVHSDCDR ASGQCVCKPG ATGLHCEKCL 1550
    PRHILMESDC VSCDDDCVGP LLNDLDSVGD AVLSLNLTGV SPAPYGILEN 1600
    LENTTKYFQR YLIKENAKKI RAEIQLEGIA EQTENLQKEL TRVLARHQKV 1650
    NAEMERTSNG TQALATFIEQ LHANIKEITE KVATLNQTAR KDFQPPVSAL 1700
    QSMHQNISSL LGLIKERNFT EMQQNATLEL KAAKDLLSRI QKRFQKPQEK 1750
    LKALKEANSL LSNHSEKLQA AEELLKEAGS KTQESNLLLL LVKANLKEEF 1800
    QEKKLRVQEE QNVTSELIAK GREWVDAAGT HTAAAQDTLT QLEHHRDELL 1850
    LWARKIRSHV DDLVMQMSKR RARDLVHRAE QHASELQSRA GALDRDLENV 1900
    RNVSLNATSA AHVHSNIQTL TEEAEMLAAD AHKTANKTDL ISESLASRGK 1950
    AVLQRSSRFL KESVGTRRKQ QGITMKLDEL KNLTSQFQES VDNITKQAND 2000
    SLAMLRESPG GMREKGRKAR ELAAAANESA VKTLEDVLAL SLRVFNTSED 2050
    LSRVNATVQE TNDLLHNSTM TTLLAGRKMK DMEMQANLLL DRLKPLKTLE 2100
    ENLSRNLSEI KLLISRARKQ AASIKVAVSA DRDCIRAYQP QTSSTNYNTL 2150
    ILNVKTQEPD NLLFYLGSSS SSDFLAVEMR RGKVAFLWDL GSGSTRLEFP 2200
    EVSINNNRWH SIYITRFGNM GSLSVKEASA AENPPVRTSK SPGPSKVLDI 2250
    NNSTLMFVGG LGGQIKKSPA VKVTHFKGCM GEAFLNGKSI GLWNYIEREG 2300
    KCNGCFGSSQ NEDSSFHFDG SGYAMVEKTL RPTVTQIVIL FSTFSPNGLL 2350
    FYLASNGTKD FLSIELVRGR VKVMVDLGSG PLTLMTDRRY NNGTWYKIAF 2400
    QRNRKQGLLA VFDAYDTSDK ETKQGETPGA ASDLNRLEKD LIYVGGLPHS 2450
    KAVRKGVSSR SYVGCIKNLE ISRSTFDLLR NSYGVRKGCA LEPIQSVSFL 2500
    RGGYVEMPPK SLSPESSLLA TFATKNSSGI LLVALGKDAE EAGGAQAHVP 2550
    FFSIMLLEGR IEVHVNSGDG TSLRKALLHA PTGSYSDGQE HSISLVRNRR 2600
    VITIQVDENS PVEMKLGPLT EGKTIDISNL YIGGLPEDKA TPMLKMRTSF 2650
    HGCIKNVVLD AQLLDFTHAT GSEQVELDTC LLAEEPMQSL HREHGELPPE 2700
    PPTLPQPELC AVDTAPGYVA GAHQFGLSQN SHLVLPLNQS DVRKRLQVQL 2750
    SIRTFASSGL IYYVAHQNQM DYATLQLQEG RLHFMFDLGK GRTKVSHPAL 2800
    LSDGKWHTVK TEYIKRKAFM TVDGQESPSV TVVGNATTLD VERKLYLGGL 2850
    PSHYRARNIG TITHSIPACI GEIMVNGQQL DKDRPLSASA VDRCYVVAQE 2900
    GTFFEGSGYA ALVKEGYKVR LDLNITLEFR TTSKNGVLLG ISSAKVDAIG 2950
    LEIVDGKVLF HVNNGAGRIT ATYQPRAARA LCDGKWHTLQ AHKSKHRIVL 3000
    TVDGNSVRAE SPHTHSTSAD TNDPIYVGGY PAHIKQNCLS SRASFRGCVR 3050
    NLRLSRGSQV QSLDLSRAFD LQGVFPHSCP GPEP 3084
    Length:3,084
    Mass (Da):338,172
    Last modified:November 1, 1990 - v1
    Checksum:iCF8E0D508046FC23
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti209 – 2091I → T(PubMed:3267223)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04064 mRNA. Translation: AAA39410.1.
    X07737 mRNA. Translation: CAA30561.1.
    X13459 mRNA. Translation: CAA31807.1.
    M36775 mRNA. Translation: AAA39406.1.
    PIRiA31771. MMMSA.
    RefSeqiNP_032506.2. NM_008480.2.
    UniGeneiMm.303386.

    Genome annotation databases

    GeneIDi16772.
    KEGGimmu:16772.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04064 mRNA. Translation: AAA39410.1 .
    X07737 mRNA. Translation: CAA30561.1 .
    X13459 mRNA. Translation: CAA31807.1 .
    M36775 mRNA. Translation: AAA39406.1 .
    PIRi A31771. MMMSA.
    RefSeqi NP_032506.2. NM_008480.2.
    UniGenei Mm.303386.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JD4 X-ray 1.90 A/B 2706-3084 [» ]
    ProteinModelPortali P19137.
    SMRi P19137. Positions 29-523, 715-1154, 1369-1558, 2140-3083.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201096. 7 interactions.
    IntActi P19137. 4 interactions.
    MINTi MINT-2635122.
    STRINGi 10090.ENSMUSP00000043957.

    PTM databases

    PhosphoSitei P19137.

    Proteomic databases

    MaxQBi P19137.
    PaxDbi P19137.
    PRIDEi P19137.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 16772.
    KEGGi mmu:16772.

    Organism-specific databases

    CTDi 284217.
    MGIi MGI:99892. Lama1.

    Phylogenomic databases

    eggNOGi NOG247347.
    HOGENOMi HOG000293201.
    HOVERGENi HBG052298.
    InParanoidi P19137.
    KOi K05637.
    PhylomeDBi P19137.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_202342. Laminin interactions.
    REACT_219680. L1CAM interactions.

    Miscellaneous databases

    EvolutionaryTracei P19137.
    NextBioi 290602.
    PROi P19137.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_LAMA1.
    Genevestigatori P19137.

    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. 2 hits.
    PF00053. Laminin_EGF. 17 hits.
    PF00054. Laminin_G_1. 4 hits.
    PF02210. Laminin_G_2. 1 hit.
    PF06008. Laminin_I. 1 hit.
    PF06009. Laminin_II. 1 hit.
    PF00055. Laminin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 15 hits.
    SM00281. LamB. 2 hits.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 5 hits.
    PROSITEi PS00022. EGF_1. 11 hits.
    PS01186. EGF_2. 3 hits.
    PS01248. EGF_LAM_1. 15 hits.
    PS50027. EGF_LAM_2. 15 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    PS51115. LAMININ_IVA. 2 hits.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains."
      Sasaki M., Kleinman H.K., Huber H., Deutzmann R., Yamada Y.
      J. Biol. Chem. 263:16536-16544(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "The N-terminus of laminin A chain is homologous to the B chains."
      Hartl L., Oberbaeumer I., Deutzmann R.
      Eur. J. Biochem. 173:629-635(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-339.
    3. "Structural study of long arm fragments of laminin. Evidence for repetitive C-terminal sequences in the A-chain, not present in the B-chains."
      Deutzmann R., Huber J., Schmetz K.A., Oberbaeumer I., Hartl L.
      Eur. J. Biochem. 177:35-45(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2538-3084, PARTIAL PROTEIN SEQUENCE.
    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: PROTEIN SEQUENCE OF 25-32, PYROGLUTAMATE FORMATION AT GLN-25.
    5. "Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands."
      Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.
      Eur. J. Biochem. 215:733-740(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBLN1.
    6. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1344; ASN-1686; ASN-1718; ASN-1725; ASN-1763; ASN-1936; ASN-2027; ASN-2046; ASN-2062; ASN-2067 AND ASN-2835.

    Entry informationi

    Entry nameiLAMA1_MOUSE
    AccessioniPrimary (citable) accession number: P19137
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3