ID A0A2K5Z9N4_MANLE Unreviewed; 3494 AA.
AC A0A2K5Z9N4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Laminin subunit alpha 5 {ECO:0000313|Ensembl:ENSMLEP00000024485.1};
GN Name=LAMA5 {ECO:0000313|Ensembl:ENSMLEP00000024485.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000024485.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000024485.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 9568.ENSMLEP00000024485; -.
DR Ensembl; ENSMLET00000048009.1; ENSMLEP00000024485.1; ENSMLEG00000036374.1.
DR GeneTree; ENSGT00940000156537; -.
DR OMA; ISHCAAH; -.
DR Proteomes; UP000233140; Unplaced.
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; 5.
DR Gene3D; 2.60.120.200; -; 5.
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 InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
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; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00180; EGF_Lam; 21.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 19.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 16.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
DR PROSITE; PS50050; TNFR_NGFR_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..200
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 260..329
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 330..374
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 395..442
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 445..489
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 490..534
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 535..579
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 580..630
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 679..731
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1341..1386
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1431..1479
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1480..1530
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1551..1733
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT REPEAT 1747..1795
FT /note="TNFR-Cys"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00206"
FT DOMAIN 1747..1795
FT /note="TNFR-Cys"
FT /evidence="ECO:0000259|PROSITE:PS50050"
FT DOMAIN 1767..1815
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1816..1871
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1872..1925
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1926..1972
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1973..2019
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2536..2729
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2743..2915
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2924..3091
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3139..3312
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 3319..3491
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1151..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2390..2503
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 297..306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 350..359
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 395..407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 418..427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 446..463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 465..474
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 490..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 510..519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 535..547
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 555..564
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 580..592
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 582..599
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 601..610
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 702..711
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1341..1353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1343..1360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1362..1371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1455..1464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1480..1492
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1482..1499
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1501..1510
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1786..1795
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1842..1851
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1897..1906
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1909..1923
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1945..1954
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1993..2002
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3494 AA; 377771 MW; 1A3BFFAF1CAD6114 CRC64;
GQYCDICTAA NSNRAHPASN AIDGTERWWQ SPPLSRGLEY NEVNVTLDLG QVFHVAYVLI
KFANSPRPDL WVLERSMDFG RTYQPWQFFA SSKRDCLERF GPQTLERITR DDAAICTTEY
SRIVPLENGE IVVSLVNGRP GAMNFSYSPL LREFTKATNV RLRFLRTNTL LGHLMGKALR
DPTVTRRYYY SIKDISIGGR CVCHGHADAC DAKDPTDPFR LQCTCQHNTC GGTCDRCCPG
FNQQPWKPAT ANSANECQSC NCHGHATDCY YDPEVDQRRA SQSLDGTYQG GGVCIDCQHH
TTGVNCERCL PGFYRSPDHP LDSPHVCRRC NCESNFTDGT CEDLTGRCYC RPNFSGERCD
VCAEGFTGFP SCYPTPSSSN DTREQVLPAG QIVNCDCSAA GTQGNACRKD PRVGRCVCKP
NFQGTHCELC VPGFYGPGSC GPPFPCSSPG VADDRCDPDT GRCRCREGFE GATCDRCAPG
YFRFPLCQLC GCSPAGTLPE GCDEAGRCPC QPGFTGPHCD QCHPGYHGFP NCQPCTCDPR
GALDQLCGAG GLCRCRPGYT GTACQECSPG FHGFPSCVPC HCSAEGSLHA ACDPRSGQCS
CRPRVMGLRC DTCVPGAYNF PYCEAGSCHP AGLALVDPAL PEAQAPCVCR ANVEGPSCDR
CKPGFWGLSP SNPEGCTRCS CDPRGTLGGV AECQPGTGQC FCKPHVCGQA CAACRDGFFG
LDQADYFGCR SCRCDAGGAL GQSCEPRTGA CRCRPNTQGP TCSRPVRDHY LPDLHHLRLE
LEEATTPEGH AVRFGFNPLE FENFSWRGYA QMAPVQPRIV ARLNLTSPDL FWLVFRYVNR
GAMSVSGRVS VREEGRSAAC TNCTAQSQPV AFPPSTEPAF VTVPQRGFGE PFVLNPGTWA
LLVEAEGVLL DYVVLLPSAY YEAALLQLRV TEACTYRPST QQSGDNCLLY THLPLDGFPS
AAGLEALCRQ DNSLPRPCPT EQLSPSHPPL VTCTGSDVDV QLQVAVPQPG RYALVVEYAN
EDARQEVGVA VHTPQRAPQQ GLLSLHPCLY STLCRGTARD TQDRLAVFHL DSEASVRLTA
EQARFYLHGV TLVPMEEFSP EFVEPRVRCI SSHGAFGPSS AACLPSRFPK PPQPIILRDC
QVIPLPPGLP LTHAQDLTPA TSPTGPQPRP PTAVDPDVEP TLLREPQATV VFTTHVPTLG
RYAFLLHGYQ PAHPTFPVEV LINAGRVWQG HANASFCPHG YGCRTLVVCE GQALLDVTHS
ELTVTVRVPE GRWLWLDYVL VVPENVYSFG YLREEPLDKS YDFISHCAAQ GYHISPGSSS
LFCRNAAASL SLFYNNGARP CGCHEVGATG PTCEPFGGQC PCRAHVIGRD CSRCATGYWG
FPSCRPCDCG ARLCDELTGQ CICPPRTVPP ECLLCQPQTF GCHPLVGCEE CNCSGPGVQE
LTDPTCDTDS GQCKCRPNVT GRRCDTCSPG FHGYPHCRPC DCHEAGTAPG VCDPLTGQCY
CKENVQGPRC DQCSLGTFSL DAANPKGCTR CFCFGATERC RSSSYTRQEF VDMEGWVLLS
TDRQVVPHER RPGTEMLRAD LRHVPEAVPE AFPELYWQAP PSYLGDRVSS YGGTLRYELH
SETQRGDVFV PTESRPDVVL QGNQMSITFL EPAYPMPGHI HRGQLQLVEG NFRHTETRNT
VSREELMMVL ASLEQLQIRA LFSQISSAVS LRRVALEVAS PAGQGTLASN VELCLCPASY
RGDSCQECAP GFYRDVKGLF LGRCVPCQCH GHSDRCLPGS GICVDCQHNT EGAQCERCQA
GFVSSREDPS APCVSCPCPL SVPSNNFAEG CVLRGGRTQC LCKPGYAGAS CERCAPGFFG
NPLVLGSSCQ PCDCSGNGDP NLLFSDCDPL TGACRGCLRH TTGPRCEICA PGFYGNALLP
GNCTRCDCAP CGTEACNPHS GQCLCKAGVT GRRCDRCQEG HFGFEGCGGC RPCACGPAAE
GSECHPQSGQ CHCRPGTMGP QCRECAPGYW GLPEQGCRRC QCPGGRCDPH TGRCTCPPGL
SGERCDTCSQ QHQVPVPGGP GDHSVHCEVC DHCVVLLLDD LERAGTLLPA IHEQLRGINA
SSVAWARLHR LNASITDLQS QLRSPLGPRH ETAQQLEVLE QQSTSLGQDA QQLDSQAGGP
PRCTQVLGRW PATGGGAGVL GLEASRQALT TPCPTELMSQ TGHLGLANAS ALSGEQLRRT
LAEQRKQELS RDNATLKATL HAASDTLASV FRLLHSLDQA KEVSAAPDPC HHPIHGQLPP
RPVGSFVCGC EQDEGLLSPL NFQDIILDIN QDRLTQRAIE ASSAYSRILQ AVQAAEDAAD
QALQQADHTW ATVVRQGLVD LARQLLANSS ALEEAVLREQ RRLGLVWAAL QGAGTQLRDV
RAKKDQLEVR IQAAQTMLAM DTDETSKKIA HAKAVAAEAQ DMAARVQSQL QAMQENVERW
QGQYEGLRGQ DLGQAVLDAG RSVSSLEKTL PQLLAKLSVL ENRGAHNASL VLSASIGRVR
QLIAQARGAA SKVKVPMKFN GRSGVQLRTP RDLADLAAYT ALKFYLQGPE PEPGQGTEDH
FVMYMGSRQA TGDYMGVSLR DKKVHWVYRL GEAGPAVLSI DEDIGEQFAA VSLDRTLQFG
HMSVTVERQM IQETKGDTVA PGAEGLLNLR PDDFVFYVGG YPSTFTPPPL LRFPGYRGCI
EMDTLNEEVV SLYNFEGTFQ LDTAVDRPCA RSKSTGDPWL TDGSYLDGTG FARISFDGQI
STTKRFEQEL RLVSYSGVLF FLKQQSQFLC LAVREGSLVL LYDFGAGLKE AVPLQTPPPL
TSASKAIQVF LLGGSRKRVL VRVERATVFS VEQDNALELA DAYYLGGAPP DQLPPSLRRL
FPMGGSVRGC VKGIKALGKY VDLKRLNTTG VSAGCTADLL VGRAMTFHGH GFLHLALSNV
APLTGDVYSG FGFHSAQDSA LLYYRASPDG PCQVSLRQGR VTLQLLRTEV IAEGGFADGA
PHYVAFYSNA TGVWLYVDDQ LQQMKPHRGP PPVPQPQPEG PPSLLLGGLP EPDTFHFSGC
ISNIFVQRLL GPQRVFDLQQ NLGSVNVSTG CAPTLQAQTL DLGPRGLRTT ARKASRRSRQ
PTQDPACMLP AHLRTTRDTY QFGGSLSSHL EFVGILAPHR NWPSLSMRVL PRSPRGLLLF
AASLRPSSPS LALFLSNGHF VAQMEGLGTR LRAQSRQRSW PGHWHKVSVH WEKNRILLVT
DGARAWSQEG PRWQHQGAEH PQPHTLFVGG LPASNHSSKL PVTVGFSGCV KRLRLHGRPL
GAPTRMAGVT PCISGPLEAG LFFPGSGGVI TLDLPGATLP DVGLELEVRP LAVTGLIFHL
GQARTPPYLQ LQVTEKQVLL RADDGAGEFS TSVTRPSVLC DGQWHRLAVM KGGNVLRLEV
DAQSNHTVGS SLAAAAGAPA PLHLGGLPEP TAMQPWPPAY RGCMRRLTVN RAPVTITRSA
EVHGAVGASG CPAA
//
