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 12-APR-2017, entry version 145. 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; Sciurognathi; 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IntAct; Q61087; 1. DR MINT; MINT-4100159; -. 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; ENSGT00780000121851; -. DR HOGENOM; HOG000113279; -. DR HOVERGEN; HBG052302; -. DR InParanoid; Q61087; -. DR KO; K06244; -. DR OMA; RVLYYAT; -. DR OrthoDB; EOG091G019I; -. 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; -. DR CleanEx; MM_LAMB3; -. DR ExpressionAtlas; Q61087; baseline and differential. DR Genevisible; Q61087; MM. DR GO; GO:0005604; C:basement membrane; IDA:MGI. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005610; C:laminin-5 complex; IDA: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 GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR Gene3D; 2.60.120.260; -; 1. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR008979; Galactose-bd-like. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR008211; Laminin_N. 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...). {ECO:0000255}. FT CARBOHYD 601 601 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 806 806 N-linked (GlcNAc...). {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 //