ID M3Y8Y0_MUSPF Unreviewed; 3008 AA.
AC M3Y8Y0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Laminin subunit alpha 5 {ECO:0000313|Ensembl:ENSMPUP00000007787.1};
GN Name=LAMA5 {ECO:0000313|Ensembl:ENSMPUP00000007787.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000007787.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000007787.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; AEYP01050460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9669.ENSMPUP00000007787; -.
DR Ensembl; ENSMPUT00000007912.1; ENSMPUP00000007787.1; ENSMPUG00000007845.1.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000156537; -.
DR HOGENOM; CLU_000301_1_0_1; -.
DR InParanoid; M3Y8Y0; -.
DR OMA; ISHCAAH; -.
DR GO; GO:0098965; C:extracellular matrix of synaptic cleft; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0043259; C:laminin-10 complex; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0030324; P:lung development; IEA:Ensembl.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IEA:Ensembl.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:0099173; P:postsynapse organization; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0036484; P:trunk neural crest cell migration; IEA:Ensembl.
DR CDD; cd00055; EGF_Lam; 19.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 19.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 20.
DR Pfam; PF02210; Laminin_G_2; 2.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00180; EGF_Lam; 22.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 18.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01248; EGF_LAM_1; 10.
DR PROSITE; PS50027; EGF_LAM_2; 16.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..26
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 86..155
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 156..200
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 222..268
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 269..319
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 321..359
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 360..404
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 405..455
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 504..556
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1166..1211
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1256..1304
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1305..1355
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1376..1554
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1588..1637
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1638..1693
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1694..1747
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1748..1794
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1795..1841
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2460..2653
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2665..2846
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2855..3008
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 980..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2127..2161
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2315..2427
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 986..1000
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 123..132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 176..185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 222..234
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 245..254
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 269..281
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 271..288
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 290..299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 335..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 360..372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 380..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 405..417
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 407..424
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 426..435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 527..536
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1166..1178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1168..1185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1187..1196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1280..1289
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1305..1317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1307..1324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1326..1335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1607..1616
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1664..1673
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1719..1728
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1731..1745
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1767..1776
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1815..1824
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3008 AA; 324968 MW; 7125F0B96D9ED32E CRC64;
MGKALRDPTV TRRYYYSIKD ISIGGRCVCH GHADVCDAQD PTDPYRLQCT CQHNTCGGSC
DRCCPGFHQR PWKPATADSA NECQSCNCHG HADDCFYDPE VDRLSASQNQ DNVYQGGGVC
IDCQHHTTGI NCERCLPGFF RAPDQPLDSP HACRRCSCES DFMDGTCEDL TGRCYCRPNF
TGEHCAACAE GFTGFPRCYP VPSFSPNDTG EQVLPAGQIV NCDCSAAGTQ GNACRRDPRL
GRCVCKPGFQ GIHCERCAPG FYGPSCQPCQ CSSPGVVDGD CDQDSGRCTC REGFEGPACD
RCAPGYFHFP LCQLCGCSPV GTLPEGCDEV GHCRCRPEFD GPHCDRCRSG YHGYPNCRAC
TCDPRGSLDQ LCRASGMCHC RPGYAGTTCQ ECSPGFHGFP DCAPCRCSAE GSLHTSCDSR
SGQCPCRPRV TGLRCDMCAP GTYNFPYCEA GSCHPAGLAP ADPSLPEAQA PCTCRAHVEG
PSCDRCKPGF WGLSPGNPEG CTRCSCDPRG TVGGLAECRP GDGQCSCKAH VCGQTCAACR
EGFFGLDQAD YFGCRSCRCD VGGALGQGCD PRTGACRCRP NTQGLTCSEP ARDHYLPDLH
DLRLELEEAA TPGGHTVRFG FNPLEFESFS WRGYAQMTPV QPRIVAKLNV TSPDLFWLVF
RYVNRGPASM SGHVSVREEG RSATCVNCTE QSQPVTFPPS TEPAFVTVPQ RGFGEPFVLN
PGAWTLLVEA EGVLLDYVVL LPSTYYEAAL LQLRVTEACA FRPPAQRSGH TCLLYSHLPL
DGFPSAAGPE ALCRQDNSLP RPCPTEQLSP SHPPLAACLG SDVDVQLQVA VPRPGHYVLV
LEYAKEEGRQ ELGVAVHTPQ RAPQQAALTL HPCPYSTLCR GTALDAQRHL AAFHLDTEAS
VRLTAEQARF FLHSVTLVPV ETFSLEFVEP RVRCVSRHGV FGPSSATCLL SRFPKPAQPI
LLRDCRVLPL APGLPLAQSQ DLIPGAPPSG PQPRPPTAVD PDVEPTLLRH PQGTVVFSTH
VPALGRYAFL LHGFQPDHPT FAVEVLISGG RVWQGHANAS FCPHGYGCRA LVVCEGRAVL
DVTDRELTVT VRVPDGRWLW LEYVLVVPEE AYSPSYLREE PLDKSYDFIS QCASRGYHIS
PTSSSPFCRD AASSLSLFYN NGARPCGCHE MGATGPTCEP FGGQCPCRAH VIGRDCSRCA
TGYWGFPSCR PCECRGRLCD ELTGQCVCPP RTVPPDCVVC QPQSFGCHPL VGCEECNCSG
PGVQELTDPT CDVDSGQCKC RPNVAGRRCD TCAPGFHGYP SCRPCDCHEA GSMPSKCDPL
TGRCHCKENV QGPRCDQCRL GTFSLDAANP KGCTRCFCFG ATERCRGSVL TRREHVDMEG
WTLLSSDRQV VPHELQAEAE LLYADLRRGF EALPELYWQA PPSYLGDRVS SYGGILRYEL
YSETQRGDVF IPTESRPDVV LQGNQMSIVF LEPVYPAPGH IHHGRLQLVE GNFRHSETHS
AVSREELMMV LAGLEQVHIR ALFSQTSAAV SLRSVALEVA GEVGGGPPAS NVELCMCPAN
YRGDSCQECA PGYYRDIKGL FLGRCVPCQC HGHSDRCLPG SGVCTGCQHH TEGDHCELCQ
PGFVRSGSED PMAPCVSCPC PLAVPSNNFA MGCVLRGGRT QCLCKPGYAG ASCERCVPGF
FGNPLVLGSS CQPCDCSGNG DPNLLFSDCD PLTGACRGCL RHTTGPRCES CAPGFFGNAL
VPGNCSRCDC STCGTETCDP HSGYCVCKAG VTGPRCDRCQ EGYFGFQDCG GCRPCACGPA
AEGSECHPQS GQCHCRPGAG GPQCRECAPG HWGLPEQGCK RCQCQGGHCD MHTGRCTCPP
GLSGERCDAC SQQHQVVVPG GPGGHGVHCE VCDHCVVLLL DDLERAGALL PAIREQLRGI
NASSVAWARL HALNASIADL QRQLQSPLGL RHETARQLET LERQTSGLGQ DTQRLDGQAT
RALAEASRLL DSTKASLGRA QALLAAIQAV DHLLSELESR MDHLFPANAS APSGEHVRRT
LAEVERLLGE MRARHLDAPR RVAEAQLDAA QRLLARVQEQ LTSHWEGNRA LAARTRDQLA
RHEAGLMDLR GTLNRAVGTT REAEELNSRN QERLEDALLR KQELSRDNAT LRATLQAASD
TLAQLSGLLH GMDQAREEYE HLAANLDGAQ TPLLEQMRAF SPAGSKVGLV EAAETHAQRL
AQLALNLSSV LRGLNQDGFI QRAVEAASAY SSVLHAVLAA EGAASQALRQ ASHTWAMVVE
RGLAPRAQEL LINGSALAET ALHEQQRLGR ARAAIQGTRT QLRDAQAKKE QLAARVQEAQ
AMLAMDTNET SRIAHAKAVA ADAQATATRV QSRLQDMRKH LQQWQDQYGG LRGQDLGQAV
LDAGRSVSTL EKTLPQLLAK LSLLENRGAR NASLALSASI GRVRELIAQA RGAASKVKVS
MKFSGHSGVR LRAPRDLSDL AAYTALKFYL QSPNRVSGQA PADRFVLYLG SRQAVGDYMG
VALRNQRVHW VYRLGEAGPA ALSVDEDIGE QFAAVSIDRT LQFGHMSVTV EKQMLHETKG
DTVAPGAEGL LNLRPDDFVF YVGGYPSHFT PPEPLRLPGY LGCIEMEALN EEVLSLYNFE
ETFQLDTTVD RPCARSKSTG DPWLTDGSYL DGSGFARISV ESQMGTTKRF EQELRLVSSS
GIVFFMQHQD QFLCLAVRKG SLLLLYDFGA GLMEATLSPA VDASLLNMTT ASKAIQVFLL
GGSRGRVSRV LVRVERNNAF SVDHSSTLEL ASAYYLGGVP PDQLPPSLRQ LFPSGGSVRG
CIKGIKAQGK YVDLKRLNTT GISSGCTADL LVGRAMTFHG DGYLSLGLPD VPPVTGHIYS
GFGFHSTQDV GLLYLKEFLD GPYQVSLQQG RVALRLPTTE VKTQGSFADG APHYVAFYSN
DTGVWLYVDD QLQQMKRHQG LPPRPQAPSE KNQVLYLGGW SESGNYSNFS GCISNVFMLR
HAGGATGV
//
