ID LMB3_MOUSE STANDARD; PRT; 1168 AA. AC Q61087; DT 01-NOV-1997 (REL. 35, CREATED) DT 01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE) DT 15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE) DE LAMININ BETA-3 CHAIN PRECURSOR (KALININ B1 CHAIN). GN LAMB3. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FVB; TISSUE=LUNG; RX MEDLINE; 95205823. RA UTANI A., KOPP J.B., KOZAK C.A., MATSUKI Y., AMIZUKA N., SUGIYAMA S., RA YAMADA Y.; 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, & ORGANIZATION OF CC 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 & THREE SHORT ARMS WITH GLOBULES AT EACH END. CC -!- SUBUNIT: THE BETA-3 CHAIN IS A SUBUNIT OF LAMININ-5 (EPILIGRIN/ CC KALININ/NICEIN). CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. 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 1 LAMININ N-TERMINAL DOMAIN (DOMAIN VI). CC -!- SIMILARITY: CONTAINS 6 LAMININ EGF-LIKE DOMAINS. 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; G1151215; -. DR MGD; MGI:99915; LAMB3. DR PROSITE; PS00022; EGF_1; 4. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS01248; LAMININ_TYPE_EGF; 3. KW GLYCOPROTEIN; BASEMENT MEMBRANE; EXTRACELLULAR MATRIX; COILED COIL; KW LAMININ EGF-LIKE DOMAIN; CELL ADHESION; REPEAT; SIGNAL. FT SIGNAL 1 17 POTENTIAL. FT CHAIN 18 1168 LAMININ BETA-3 CHAIN. FT DOMAIN 18 249 LAMININ N-TERMINAL (DOMAIN VI). FT DOMAIN 250 575 6 X LAMININ EGF-LIKE REPEATS (DOMAIN FT V/III). 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 531 575 LAMININ EGF-LIKE 6. FT DOMAIN 576 781 DOMAIN II. FT DOMAIN 782 812 DOMAIN ALPHA. FT DOMAIN 813 1168 DOMAIN I. FT DOMAIN 732 754 COILED COIL (POTENTIAL). FT DOMAIN 827 879 COILED COIL (POTENTIAL). FT DOMAIN 944 1129 COILED COIL (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). FT CARBOHYD 220 220 POTENTIAL. FT CARBOHYD 601 601 POTENTIAL. FT CARBOHYD 806 806 POTENTIAL. SQ SEQUENCE 1168 AA; 128996 MW; 0FBE0A4A CRC32; 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 //