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 02-OCT-2024, entry version 187. 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. 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 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.ENSMUSP00000142053; -. DR GlyCosmos; Q61087; 3 sites, No reported glycans. DR GlyGen; Q61087; 3 sites. DR iPTMnet; Q61087; -. DR PhosphoSitePlus; Q61087; -. DR PaxDb; 10090-ENSMUSP00000016315; -. DR PeptideAtlas; Q61087; -. DR ProteomicsDB; 264831; -. DR Antibodypedia; 1958; 438 antibodies from 28 providers. DR DNASU; 16780; -. DR Ensembl; ENSMUST00000016315.16; ENSMUSP00000016315.10; ENSMUSG00000026639.19. DR Ensembl; ENSMUST00000159955.2; ENSMUSP00000123875.2; ENSMUSG00000026639.19. DR Ensembl; ENSMUST00000194677.6; ENSMUSP00000142053.2; ENSMUSG00000026639.19. DR GeneID; 16780; -. DR KEGG; mmu:16780; -. DR UCSC; uc007eee.1; mouse. DR AGR; MGI:99915; -. 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; RCLCLPH; -. DR OrthoDB; 90222at2759; -. DR PhylomeDB; Q61087; -. DR TreeFam; TF352481; -. DR BioGRID-ORCS; 16780; 1 hit in 80 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 148 other cell types or tissues. DR ExpressionAtlas; Q61087; baseline and differential. 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:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central. DR GO; GO:0007411; P:axon guidance; 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 Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 2.10.25.10; Laminin; 4. DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1. DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR050440; Laminin/Netrin_ECM. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR002049; LE_dom. DR PANTHER; PTHR10574:SF268; LAMININ SUBUNIT BETA-3; 1. DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1. DR Pfam; PF00053; Laminin_EGF; 6. DR Pfam; PF00055; Laminin_N; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00181; EGF; 4. DR SMART; SM00180; EGF_Lam; 6. DR SMART; SM00136; LamNT; 1. DR SUPFAM; SSF57196; EGF/Laminin; 5. 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 //