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Q61087

- LAMB3_MOUSE

UniProt

Q61087 - LAMB3_MOUSE

Protein

Laminin subunit beta-3

Gene

Lamb3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (27 Jul 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 - Biological processi

    1. brown fat cell differentiation Source: MGI
    2. cell adhesion Source: UniProtKB-KW

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_196595. Anchoring fibril formation.
    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 beta-3
    Alternative name(s):
    Epiligrin subunit bata
    Kalinin B1 chain
    Kalinin subunit beta
    Laminin-5 subunit beta
    Nicein subunit beta
    Gene namesi
    Name:Lamb3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:99915. Lamb3.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: MGI
    2. extracellular region Source: Reactome
    3. 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 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 11681151Laminin subunit beta-3PRO_0000017072Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi250 ↔ 259PROSITE-ProRule annotation
    Disulfide bondi252 ↔ 276PROSITE-ProRule annotation
    Disulfide bondi278 ↔ 287PROSITE-ProRule annotation
    Disulfide bondi290 ↔ 310PROSITE-ProRule annotation
    Disulfide bondi313 ↔ 322PROSITE-ProRule annotation
    Disulfide bondi315 ↔ 340PROSITE-ProRule annotation
    Disulfide bondi343 ↔ 352PROSITE-ProRule annotation
    Disulfide bondi355 ↔ 373PROSITE-ProRule annotation
    Disulfide bondi376 ↔ 389PROSITE-ProRule annotation
    Disulfide bondi378 ↔ 396PROSITE-ProRule annotation
    Disulfide bondi398 ↔ 407PROSITE-ProRule annotation
    Disulfide bondi410 ↔ 425PROSITE-ProRule annotation
    Disulfide bondi428 ↔ 441PROSITE-ProRule annotation
    Disulfide bondi430 ↔ 448PROSITE-ProRule annotation
    Disulfide bondi450 ↔ 459PROSITE-ProRule annotation
    Disulfide bondi462 ↔ 475PROSITE-ProRule annotation
    Disulfide bondi478 ↔ 490PROSITE-ProRule annotation
    Disulfide bondi480 ↔ 497PROSITE-ProRule annotation
    Disulfide bondi499 ↔ 508PROSITE-ProRule annotation
    Disulfide bondi516 ↔ 528PROSITE-ProRule annotation
    Disulfide bondi531 ↔ 543PROSITE-ProRule annotation
    Disulfide bondi533 ↔ 550PROSITE-ProRule annotation
    Disulfide bondi552 ↔ 561PROSITE-ProRule annotation
    Disulfide bondi564 ↔ 575PROSITE-ProRule annotation
    Disulfide bondi578 – 578InterchainCurated
    Disulfide bondi581 – 581InterchainCurated
    Glycosylationi601 – 6011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi806 – 8061N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1167 – 1167InterchainCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ61087.
    PRIDEiQ61087.

    PTM databases

    PhosphoSiteiQ61087.

    Expressioni

    Tissue specificityi

    Found in the basement membranes (major component).

    Gene expression databases

    BgeeiQ61087.
    CleanExiMM_LAMB3.
    GenevestigatoriQ61087.

    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. Beta-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Interacts with ECM1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ61087. 1 interaction.
    MINTiMINT-4100159.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61087.
    SMRiQ61087. Positions 20-563.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 249228Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini250 – 31263Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini313 – 37563Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini376 – 42752Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini428 – 47750Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini478 – 53053Laminin EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini531 – 57747Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni576 – 781206Domain IIAdd
    BLAST
    Regioni782 – 81231Domain alphaAdd
    BLAST
    Regioni813 – 1168356Domain IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili732 – 75423Sequence AnalysisAdd
    BLAST
    Coiled coili827 – 87953Sequence AnalysisAdd
    BLAST
    Coiled coili944 – 1129186Sequence AnalysisAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 6 laminin EGF-like 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

    eggNOGiNOG289025.
    GeneTreeiENSGT00740000115270.
    HOGENOMiHOG000113279.
    HOVERGENiHBG052302.
    InParanoidiQ91V90.
    KOiK06244.
    OMAiRSQMEED.
    OrthoDBiEOG77WWBQ.
    TreeFamiTF352481.

    Family and domain databases

    InterProiIPR002049. EGF_laminin.
    IPR008211. Laminin_N.
    [Graphical view]
    PfamiPF00053. Laminin_EGF. 6 hits.
    PF00055. Laminin_N. 1 hit.
    [Graphical view]
    SMARTiSM00180. EGF_Lam. 6 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 5 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 4 hits.
    PS50027. EGF_LAM_2. 6 hits.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q61087-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAFFLLWLA LPGFLCAQQA CSRGACYPPV GDLLIGRTQL LRASSTCGLT     50
    KPETYCTQYG QWQMKCCKCD SRLPRNYNSH RVENVASSSG PMRWWQSQND 100
    VSPVSLQLDL DKRMQLQDIM MDFKGLTPAG MLIERSSDFG KTWRVYQYLA 150
    TDCASTFPQV HQGQPKNWQD VRCRPLSQRP NGHLTGGKVQ LNLMDLASAI 200
    PASQSKKIQE LGDITNLRVN FTKLAPVPQR GSYPPSAYFA VSQLRLQGSC 250
    FCHGHADRCA PNPGGSTTAV QVNNVCVCQH NTAGPNCDRC APFYNNRPWR 300
    PAEGQDTHEC QRCDCNGHSE TCHFDPAVFA ASQGTNGGVC DNCRDHTEGK 350
    NCERCQLHYF RNRRPSAPIH ETCIPCECDP DGAVQGAPCD RLTGQCVCKE 400
    YVQGERCDLC KPGFTGLTFA NPKGCHACDC SILGARKDMP CEEETGRCLC 450
    LPNVVGPKCD QCAPSHWKLA SGLGCEPCAC DPRNSLSSQC NQFTGQCPCR 500
    EGFGGLTCSS AAIRQCPDQT YGHVATGCRA CDCDFRGTEG PGCDKASGRC 550
    LCRPGFTGPR CDQCQRGHCD RYPVCVACHS CFQAYDTDLQ EQARRLHSLR 600
    NATEGLWTGT GLEDHGLASR LLDAKSKIEQ IRQILEGTSV TEQDVAQVAN 650
    GILSIRRTLQ GLPLDLPLEE EMESFSGDLG NLDRSFSRLL LMYRSKKEQF 700
    EKLSSEDPSG AFRMLTMAYE QSSRAAQQVS DSSSLLSQLR DSRREAEGLE 750
    RQAGGGGTGG AQLMALRLEM ASLPDLTPTI NKLCGRSRQT ACTPGDCPGE 800
    LCPQDNGTAC GSHCRGALPR AKGAFHMAGR VAEQLRNFNT QLQQTRQMIR 850
    AAEEAASRVQ ADAQRLETQV STSRLLMEED VQRTRLLIQQ VRGFLTDPDT 900
    DAATIQQVSE AVLALWLPTD SATVLRKMKE IQAIAARLPN VDSVLSQTKQ 950
    DIARARRLQA EAEQARSRAH AVEGQVDDVV GNLRQGTVAL QEAQDTMQGT 1000
    GRSLRLIQER VGEVQQVLVP AERLVKGMKE QMSGFWARMK ELRRQAQEEQ 1050
    AQAMQARQLA EGASQQAMNA QEGFKRLKQK YTELKDRLGQ SPVLGEQGNR 1100
    ILSIKMEAEE LFGETMEMMD KMKDMESELL RGSQAIMLRS ADLSGLEKRV 1150
    EQIRSYINGR VLYYATCK 1168
    Length:1,168
    Mass (Da):128,900
    Last modified:July 27, 2011 - v2
    Checksum:i66EB2BE1AA232215
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341L → F in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti271 – 2711Q → R in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti284 – 2841G → A in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti320 – 3201E → L in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti354 – 3541R → P in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti361 – 3611R → W in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti420 – 4201A → D in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti525 – 5251A → P in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti542 – 5421G → A in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti646 – 6461A → P in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti1079 – 10791Q → P in AAA85255. (PubMed:7898049)Curated
    Sequence conflicti1115 – 11151T → S in AAA85255. (PubMed:7898049)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43298 mRNA. Translation: AAA85255.1.
    AK155769 mRNA. Translation: BAE33428.1.
    CH466555 Genomic DNA. Translation: EDL12945.1.
    CH466555 Genomic DNA. Translation: EDL12946.1.
    BC008516 mRNA. Translation: AAH08516.1.
    CCDSiCCDS15637.1.
    RefSeqiNP_001264857.1. NM_001277928.1.
    NP_032510.2. NM_008484.2.
    XP_006497295.1. XM_006497232.1.
    XP_006497296.1. XM_006497233.1.
    UniGeneiMm.435441.

    Genome annotation databases

    EnsembliENSMUST00000016315; ENSMUSP00000016315; ENSMUSG00000026639.
    ENSMUST00000159955; ENSMUSP00000123875; ENSMUSG00000026639.
    GeneIDi16780.
    KEGGimmu:16780.
    UCSCiuc007eee.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43298 mRNA. Translation: AAA85255.1 .
    AK155769 mRNA. Translation: BAE33428.1 .
    CH466555 Genomic DNA. Translation: EDL12945.1 .
    CH466555 Genomic DNA. Translation: EDL12946.1 .
    BC008516 mRNA. Translation: AAH08516.1 .
    CCDSi CCDS15637.1.
    RefSeqi NP_001264857.1. NM_001277928.1.
    NP_032510.2. NM_008484.2.
    XP_006497295.1. XM_006497232.1.
    XP_006497296.1. XM_006497233.1.
    UniGenei Mm.435441.

    3D structure databases

    ProteinModelPortali Q61087.
    SMRi Q61087. Positions 20-563.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q61087. 1 interaction.
    MINTi MINT-4100159.

    PTM databases

    PhosphoSitei Q61087.

    Proteomic databases

    PaxDbi Q61087.
    PRIDEi Q61087.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000016315 ; ENSMUSP00000016315 ; ENSMUSG00000026639 .
    ENSMUST00000159955 ; ENSMUSP00000123875 ; ENSMUSG00000026639 .
    GeneIDi 16780.
    KEGGi mmu:16780.
    UCSCi uc007eee.1. mouse.

    Organism-specific databases

    CTDi 3914.
    MGIi MGI:99915. Lamb3.

    Phylogenomic databases

    eggNOGi NOG289025.
    GeneTreei ENSGT00740000115270.
    HOGENOMi HOG000113279.
    HOVERGENi HBG052302.
    InParanoidi Q91V90.
    KOi K06244.
    OMAi RSQMEED.
    OrthoDBi EOG77WWBQ.
    TreeFami TF352481.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi LAMB3. mouse.
    NextBioi 290632.
    PROi Q61087.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61087.
    CleanExi MM_LAMB3.
    Genevestigatori Q61087.

    Family and domain databases

    InterProi IPR002049. EGF_laminin.
    IPR008211. Laminin_N.
    [Graphical view ]
    Pfami PF00053. Laminin_EGF. 6 hits.
    PF00055. Laminin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 6 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 5 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 4 hits.
    PS50027. EGF_LAM_2. 6 hits.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse kalinin B1 (laminin beta 3 chain): cloning and tissue distribution."
      Utani A., Kopp J.B., Kozak C.A., Matsuki Y., Amizuka N., Sugiyama S., Yamada Y.
      Lab. Invest. 72:300-310(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: FVB.
      Tissue: Lung.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiLAMB3_MOUSE
    AccessioniPrimary (citable) accession number: Q61087
    Secondary accession number(s): Q91V90
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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