ID LAMB3_MOUSE STANDARD; PRT; 1168 AA. AC Q61087; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 07-MAR-2006, entry version 47. DE Laminin beta-3 chain precursor (Laminin 5 beta 3) (Kalinin B1 chain). 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=FVB; TISSUE=Lung; RX MEDLINE=95205823; 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). 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. The beta-3 chain is a subunit of laminin-5 CC (epiligrin/kalinin/nicein). CC -!- SUBCELLULAR LOCATION: Secreted protein; extracellular space. 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 -!- SIMILARITY: Contains 6 laminin EGF-like domains. CC -!- SIMILARITY: Contains 1 laminin N-terminal domain. 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 HSSP; P02468; 1NPE. DR Ensembl; ENSMUSG00000026639; Mus musculus. DR MGI; MGI:99915; Lamb3. DR GO; GO:0005615; C:extracellular space; TAS. DR InterPro; IPR006210; EGF. DR InterPro; IPR002049; EGF_laminin. DR InterPro; IPR013032; EGF_like_reg. DR InterPro; IPR008211; Laminin_N. DR Pfam; PF00053; Laminin_EGF; 6. DR Pfam; PF00055; Laminin_N; 1. DR PRINTS; PR00011; EGFLAMININ. DR SMART; SM00181; EGF; 2. DR SMART; SM00180; EGF_Lam; 6. DR SMART; SM00136; LamNT; 1. DR PROSITE; PS00022; EGF_1; 4. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS01248; EGF_LAM_1; 3. DR PROSITE; PS50027; EGF_LAM_2; 6. DR PROSITE; PS51117; LAMININ_NTER; 1. KW Basement membrane; Cell adhesion; Coiled coil; Extracellular matrix; KW Glycoprotein; Laminin EGF-like domain; Repeat; Signal. FT SIGNAL 1 17 Potential. FT CHAIN 18 1168 Laminin beta-3 chain. FT /FTId=PRO_0000017072. FT DOMAIN 22 249 Laminin N-terminal. FT DOMAIN 250 312 Laminin EGF-like 1. FT DOMAIN 313 375 Laminin EGF-like 2. FT DOMAIN 376 427 Laminin EGF-like 3. FT DOMAIN 428 477 Laminin EGF-like 4. FT DOMAIN 478 530 Laminin EGF-like 5. FT DOMAIN 531 577 Laminin EGF-like 6. FT REGION 576 781 Domain II. FT REGION 782 812 Domain alpha. FT REGION 813 1168 Domain I. FT COILED 732 754 Potential. FT COILED 827 879 Potential. FT COILED 944 1129 Potential. FT CARBOHYD 220 220 N-linked (GlcNAc...) (Potential). FT CARBOHYD 601 601 N-linked (GlcNAc...) (Potential). FT CARBOHYD 806 806 N-linked (GlcNAc...) (Potential). FT DISULFID 250 259 By similarity. FT DISULFID 252 276 By similarity. FT DISULFID 278 287 By similarity. FT DISULFID 290 310 By similarity. FT DISULFID 313 322 By similarity. FT DISULFID 315 340 By similarity. FT DISULFID 343 352 By similarity. FT DISULFID 355 373 By similarity. FT DISULFID 376 389 By similarity. FT DISULFID 378 396 By similarity. FT DISULFID 398 407 By similarity. FT DISULFID 410 425 By similarity. FT DISULFID 428 441 By similarity. FT DISULFID 430 448 By similarity. FT DISULFID 450 459 By similarity. FT DISULFID 462 475 By similarity. FT DISULFID 478 490 By similarity. FT DISULFID 480 497 By similarity. FT DISULFID 499 508 By similarity. FT DISULFID 516 528 By similarity. FT DISULFID 531 543 By similarity. FT DISULFID 533 550 By similarity. FT DISULFID 552 561 By similarity. FT DISULFID 564 575 By similarity. FT DISULFID 578 578 Interchain (Probable). FT DISULFID 581 581 Interchain (Probable). FT DISULFID 1167 1167 Interchain (Probable). SQ SEQUENCE 1168 AA; 128996 MW; 31E22FA8ADD6EBC0 CRC64; MTAFFLLWLA LPGFLCAQQA CSRGACYPPV GDLFIGRTQL LRASSTCGLT KPETYCTQYG QWQMKCCKCD SRLPRNYNSH RVENVASSSG PMRWWQSQND VSPVSLQLDL DKRMQLQDIM MDFKGLTPAG MLIERSSDFG KTWRVYQYLA TDCASTFPQV HQGQPKNWQD VRCRPLSQRP NGHLTGGKVQ LNLMDLASAI PASQSKKIQE LGDITNLRVN FTKLAPVPQR GSYPPSAYFA VSQLRLQGSC FCHGHADRCA PNPGGSTTAV RVNNVCVCQH NTAAPNCDRC APFYNNRPWR PAEGQDTHEC QRCDCNGHSL TCHFDPAVFA ASQGTNGGVC DNCRDHTEGK NCEPCQLHYF WNRRPSAPIH ETCIPCECDP DGAVQGAPCD RLTGQCVCKE YVQGERCDLC KPGFTGLTFD NPKGCHACDC SILGARKDMP CEEETGRCLC LPNVVGPKCD QCAPSHWKLA SGLGCEPCAC DPRNSLSSQC NQFTGQCPCR EGFGGLTCSS AAIRQCPDQT YGHVPTGCRA CDCDFRGTEG PACDKASGRC LCRPGFTGPR CDQCQRGHCD RYPVCVACHS CFQAYDTDLQ EQARRLHSLR NATEGLWTGT GLEDHGLASR LLDAKSKIEQ IRQILEGTSV TEQDVPQVAN 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 QEGFKRLKPK YTELKDRLGQ SPVLGEQGNR ILSIKMEAEE LFGESMEMMD KMKDMESELL RGSQAIMLRS ADLSGLEKRV EQIRSYINGR VLYYATCK //