GenomeNet

Database: UniProt
Entry: Q61087
LinkDB: Q61087
Original site: Q61087 
ID   LAMB3_MOUSE             Reviewed;        1168 AA.
AC   Q61087; Q91V90;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   13-FEB-2019, entry version 159.
DE   RecName: Full=Laminin subunit beta-3;
DE   AltName: Full=Epiligrin subunit bata;
DE   AltName: Full=Kalinin B1 chain;
DE   AltName: Full=Kalinin subunit beta;
DE   AltName: Full=Laminin-5 subunit beta;
DE   AltName: Full=Nicein subunit beta;
DE   Flags: Precursor;
GN   Name=Lamb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/NJ; TISSUE=Lung;
RX   PubMed=7898049;
RA   Utani A., Kopp J.B., Kozak C.A., Matsuki Y., Amizuka N., Sugiyama S.,
RA   Yamada Y.;
RT   "Mouse kalinin B1 (laminin beta 3 chain): cloning and tissue
RT   distribution.";
RL   Lab. Invest. 72:300-310(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin
CC       is thought to mediate the attachment, migration and organization
CC       of cells into tissues during embryonic development by interacting
CC       with other extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound
CC       to each other by disulfide bonds into a cross-shaped molecule
CC       comprising one long and three short arms with globules at each
CC       end. Beta-3 is a subunit of laminin-5 (laminin-332 or
CC       epiligrin/kalinin/nicein). Interacts with ECM1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- TISSUE SPECIFICITY: Found in the basement membranes (major
CC       component).
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact
CC       with other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domain VI is globular.
DR   EMBL; U43298; AAA85255.1; -; mRNA.
DR   EMBL; AK155769; BAE33428.1; -; mRNA.
DR   EMBL; CH466555; EDL12945.1; -; Genomic_DNA.
DR   EMBL; CH466555; EDL12946.1; -; Genomic_DNA.
DR   EMBL; BC008516; AAH08516.1; -; mRNA.
DR   CCDS; CCDS15637.1; -.
DR   RefSeq; NP_001264857.1; NM_001277928.1.
DR   RefSeq; NP_032510.2; NM_008484.2.
DR   RefSeq; XP_006497295.1; XM_006497232.1.
DR   RefSeq; XP_006497296.1; XM_006497233.2.
DR   UniGene; Mm.435441; -.
DR   ProteinModelPortal; Q61087; -.
DR   SMR; Q61087; -.
DR   ComplexPortal; CPX-3012; Laminin-332 complex variant A.
DR   ComplexPortal; CPX-3164; Laminin-332 complex variant B.
DR   IntAct; Q61087; 1.
DR   MINT; Q61087; -.
DR   STRING; 10090.ENSMUSP00000016315; -.
DR   iPTMnet; Q61087; -.
DR   PhosphoSitePlus; Q61087; -.
DR   MaxQB; Q61087; -.
DR   PaxDb; Q61087; -.
DR   PeptideAtlas; Q61087; -.
DR   PRIDE; Q61087; -.
DR   Ensembl; ENSMUST00000016315; ENSMUSP00000016315; ENSMUSG00000026639.
DR   Ensembl; ENSMUST00000159955; ENSMUSP00000123875; ENSMUSG00000026639.
DR   Ensembl; ENSMUST00000194677; ENSMUSP00000142053; ENSMUSG00000026639.
DR   GeneID; 16780; -.
DR   KEGG; mmu:16780; -.
DR   UCSC; uc007eee.1; mouse.
DR   CTD; 3914; -.
DR   MGI; MGI:99915; Lamb3.
DR   eggNOG; KOG0994; Eukaryota.
DR   eggNOG; ENOG410XPEG; LUCA.
DR   GeneTree; ENSGT00940000160731; -.
DR   HOGENOM; HOG000113279; -.
DR   HOVERGEN; HBG052302; -.
DR   InParanoid; Q61087; -.
DR   KO; K06244; -.
DR   OMA; ETMEMMD; -.
DR   OrthoDB; 88170at2759; -.
DR   TreeFam; TF352481; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-MMU-2214320; Anchoring fibril formation.
DR   Reactome; R-MMU-3000157; Laminin interactions.
DR   Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR   Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR   ChiTaRS; Lamb3; mouse.
DR   PRO; PR:Q61087; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026639; Expressed in 157 organ(s), highest expression level in molar tooth.
DR   ExpressionAtlas; Q61087; baseline and differential.
DR   Genevisible; Q61087; MM.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005610; C:laminin-5 complex; IDA:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   Pfam; PF00053; Laminin_EGF; 6.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00180; EGF_Lam; 6.
DR   SMART; SM00136; LamNT; 1.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 4.
DR   PROSITE; PS50027; EGF_LAM_2; 6.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   1: Evidence at protein level;
KW   Basement membrane; Cell adhesion; Coiled coil; Complete proteome;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18   1168       Laminin subunit beta-3.
FT                                /FTId=PRO_0000017072.
FT   DOMAIN       22    249       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      250    312       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      313    375       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      376    427       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      428    477       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      478    530       Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      531    577       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   REGION      576    781       Domain II.
FT   REGION      782    812       Domain alpha.
FT   REGION      813   1168       Domain I.
FT   COILED      732    754       {ECO:0000255}.
FT   COILED      827    879       {ECO:0000255}.
FT   COILED      944   1129       {ECO:0000255}.
FT   CARBOHYD    220    220       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    601    601       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    806    806       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    250    259       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    252    276       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    278    287       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    290    310       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    313    322       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    315    340       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    343    352       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    355    373       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    376    389       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    378    396       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    398    407       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    410    425       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    428    441       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    430    448       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    450    459       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    462    475       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    478    490       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    480    497       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    499    508       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    516    528       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    531    543       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    533    550       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    552    561       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    564    575       {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DISULFID    578    578       Interchain. {ECO:0000305}.
FT   DISULFID    581    581       Interchain. {ECO:0000305}.
FT   DISULFID   1167   1167       Interchain. {ECO:0000305}.
FT   CONFLICT     34     34       L -> F (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT    271    271       Q -> R (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT    284    284       G -> A (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT    320    320       E -> L (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT    354    354       R -> P (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT    361    361       R -> W (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT    420    420       A -> D (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT    525    525       A -> P (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT    542    542       G -> A (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT    646    646       A -> P (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT   1079   1079       Q -> P (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
FT   CONFLICT   1115   1115       T -> S (in Ref. 1; AAA85255).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1168 AA;  128900 MW;  66EB2BE1AA232215 CRC64;
     MTAFFLLWLA LPGFLCAQQA CSRGACYPPV GDLLIGRTQL LRASSTCGLT KPETYCTQYG
     QWQMKCCKCD SRLPRNYNSH RVENVASSSG PMRWWQSQND VSPVSLQLDL DKRMQLQDIM
     MDFKGLTPAG MLIERSSDFG KTWRVYQYLA TDCASTFPQV HQGQPKNWQD VRCRPLSQRP
     NGHLTGGKVQ LNLMDLASAI PASQSKKIQE LGDITNLRVN FTKLAPVPQR GSYPPSAYFA
     VSQLRLQGSC FCHGHADRCA PNPGGSTTAV QVNNVCVCQH NTAGPNCDRC APFYNNRPWR
     PAEGQDTHEC QRCDCNGHSE TCHFDPAVFA ASQGTNGGVC DNCRDHTEGK NCERCQLHYF
     RNRRPSAPIH ETCIPCECDP DGAVQGAPCD RLTGQCVCKE YVQGERCDLC KPGFTGLTFA
     NPKGCHACDC SILGARKDMP CEEETGRCLC LPNVVGPKCD QCAPSHWKLA SGLGCEPCAC
     DPRNSLSSQC NQFTGQCPCR EGFGGLTCSS AAIRQCPDQT YGHVATGCRA CDCDFRGTEG
     PGCDKASGRC LCRPGFTGPR CDQCQRGHCD RYPVCVACHS CFQAYDTDLQ EQARRLHSLR
     NATEGLWTGT GLEDHGLASR LLDAKSKIEQ IRQILEGTSV TEQDVAQVAN GILSIRRTLQ
     GLPLDLPLEE EMESFSGDLG NLDRSFSRLL LMYRSKKEQF EKLSSEDPSG AFRMLTMAYE
     QSSRAAQQVS DSSSLLSQLR DSRREAEGLE RQAGGGGTGG AQLMALRLEM ASLPDLTPTI
     NKLCGRSRQT ACTPGDCPGE LCPQDNGTAC GSHCRGALPR AKGAFHMAGR VAEQLRNFNT
     QLQQTRQMIR AAEEAASRVQ ADAQRLETQV STSRLLMEED VQRTRLLIQQ VRGFLTDPDT
     DAATIQQVSE AVLALWLPTD SATVLRKMKE IQAIAARLPN VDSVLSQTKQ DIARARRLQA
     EAEQARSRAH AVEGQVDDVV GNLRQGTVAL QEAQDTMQGT GRSLRLIQER VGEVQQVLVP
     AERLVKGMKE QMSGFWARMK ELRRQAQEEQ AQAMQARQLA EGASQQAMNA QEGFKRLKQK
     YTELKDRLGQ SPVLGEQGNR ILSIKMEAEE LFGETMEMMD KMKDMESELL RGSQAIMLRS
     ADLSGLEKRV EQIRSYINGR VLYYATCK
//
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