LAMB3_MOUSE
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 03-AUG-2022, entry version 175.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT 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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Beta-3 is a
CC subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).
CC Interacts with ECM1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- TISSUE SPECIFICITY: Found in the basement membranes (major component).
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC other laminin chains to form a coiled coil structure.
CC -!- DOMAIN: Domain VI is globular.
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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 AlphaFoldDB; Q61087; -.
DR SMR; Q61087; -.
DR BioGRID; 201103; 3.
DR ComplexPortal; CPX-3012; Laminin-332 complex variant A.
DR ComplexPortal; CPX-3164; Laminin-332 complex variant B.
DR STRING; 10090.ENSMUSP00000016315; -.
DR GlyGen; Q61087; 3 sites.
DR iPTMnet; Q61087; -.
DR PhosphoSitePlus; Q61087; -.
DR MaxQB; Q61087; -.
DR PaxDb; Q61087; -.
DR PeptideAtlas; Q61087; -.
DR PRIDE; Q61087; -.
DR ProteomicsDB; 264831; -.
DR Antibodypedia; 1958; 391 antibodies from 28 providers.
DR DNASU; 16780; -.
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 VEuPathDB; HostDB:ENSMUSG00000026639; -.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000160731; -.
DR HOGENOM; CLU_001560_0_0_1; -.
DR InParanoid; Q61087; -.
DR OMA; WKVYQYL; -.
DR OrthoDB; 88170at2759; -.
DR PhylomeDB; Q61087; -.
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 BioGRID-ORCS; 16780; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Lamb3; mouse.
DR PRO; PR:Q61087; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61087; protein.
DR Bgee; ENSMUSG00000026639; Expressed in molar tooth and 147 other tissues.
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:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005610; C:laminin-5 complex; IDA:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 6.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
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; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1168
FT /note="Laminin subunit beta-3"
FT /id="PRO_0000017072"
FT DOMAIN 22..249
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 250..312
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 313..375
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 376..427
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 428..477
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 478..530
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 531..577
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 576..781
FT /note="Domain II"
FT REGION 723..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..812
FT /note="Domain alpha"
FT REGION 813..1168
FT /note="Domain I"
FT COILED 732..754
FT /evidence="ECO:0000255"
FT COILED 827..879
FT /evidence="ECO:0000255"
FT COILED 944..1129
FT /evidence="ECO:0000255"
FT COMPBIAS 723..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 250..259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 252..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 278..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 290..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 313..322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 315..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 343..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 355..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 376..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 378..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 398..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 410..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 428..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 430..448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 450..459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 462..475
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 478..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 480..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 499..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 516..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 531..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 533..550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 552..561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 564..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 578
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 581
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1167
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="L -> F (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="Q -> R (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="G -> A (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="E -> L (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="R -> P (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="R -> W (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="A -> D (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="A -> P (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="G -> A (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="A -> P (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 1079
FT /note="Q -> P (in Ref. 1; AAA85255)"
FT /evidence="ECO:0000305"
FT CONFLICT 1115
FT /note="T -> S (in Ref. 1; AAA85255)"
FT /evidence="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
