ID A0A2K5LWF1_CERAT Unreviewed; 3079 AA.
AC A0A2K5LWF1;
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 1 {ECO:0000313|Ensembl:ENSCATP00000017276.1};
GN Name=LAMA1 {ECO:0000313|Ensembl:ENSCATP00000017276.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000017276.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000017276.1}
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 RefSeq; XP_011901319.1; XM_012045929.1.
DR STRING; 9531.ENSCATP00000017276; -.
DR Ensembl; ENSCATT00000041442.1; ENSCATP00000017276.1; ENSCATG00000032537.1.
DR GeneID; 105579298; -.
DR KEGG; caty:105579298; -.
DR CTD; 284217; -.
DR GeneTree; ENSGT00940000157124; -.
DR OMA; TVRQHVH; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000032537; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005606; C:laminin-1 complex; IEA:Ensembl.
DR GO; GO:0005608; C:laminin-3 complex; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; 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:0061304; P:retinal blood vessel morphogenesis; IEA:Ensembl.
DR CDD; cd00055; EGF_Lam; 14.
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; 14.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
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; 2.
DR Pfam; PF00053; Laminin_EGF; 17.
DR Pfam; PF00054; Laminin_G_1; 5.
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; 12.
DR SMART; SM00180; EGF_Lam; 17.
DR SMART; SM00281; LamB; 2.
DR SMART; SM00282; LamG; 5.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 15.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 11.
DR PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR PROSITE; PS51115; LAMININ_IVA; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..3079
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014462252"
FT DOMAIN 22..273
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 401..457
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 458..506
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 527..712
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 746..794
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 853..905
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 906..954
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 955..1001
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1002..1047
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1048..1093
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1094..1153
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1164..1365
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 1407..1455
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1513..1559
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2121..2301
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2309..2485
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2490..2677
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2717..2889
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2894..3074
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 2412..2433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1719..1778
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2412..2427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 401..413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 433..442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 477..486
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 764..773
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 877..886
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 889..903
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 906..918
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 908..925
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 927..936
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 955..967
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 975..984
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1020..1029
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1048..1060
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1050..1067
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1069..1078
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1094..1106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1124..1133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1426..1435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1513..1525
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1515..1532
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1534..1543
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2650..2677
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3079 AA; 337561 MW; E7B7C87B101684F3 CRC64;
MRGGGAWGVL LASLLWVAAR CQQRGLFPAI LNLASNADIS TNATCGEKGP EMFCKLVEHV
PGRPVRNPQC RICDGNSANP RERHPISHAI DGTNNWWQSP SIQNGREYHW VTITLDLRQV
FQVAYVIIKA ANAPRPGNWI LERSLDGTTF SPWQYYAVSD SECLSRYNIT PRRGPPTYRA
DDEVICTSYY SRLVPLEHGE IHTSLINGRP SADDLSPKLL EFTSARYIRL RLQRIRTLNA
DLMTLSHREP KDLDPIVTRR YYYSIKDISV GGMCICYGHA SSCPWDETTK KLQCQCEHNT
CGESCNRCCP GYHQRPWRPG TVSSGNTCEA CNCHNKAKDC YYDESVAKQK KSLNTAGQFR
GGGVCTNCLQ NTMGINCETC IDGYYRPHKV SPYEDEPCRP CDCDPVGSLS SVCVKDELHS
DLRNGKGPGQ CPCKEGYAGE KCDRCQLGYK DYPACVSCGC NPVGSASDEP CTGPCVCKEN
VEGKACDRCK PGFYNLKEKN PQGCSECFCF GVSDVCSSLS WPVGQVSNMS GWLVTDLISP
RRIPSQRDAL GGRHQVSINN TAVMQRLAPK YYWAAPEAYL GNKLTAFGGF LKYTVSYDIP
VETVDSNLMS HADVIIKGNR LTLSTQAEGL SLQPYEEYLN VVRLVPENFR DFHSKRQIDR
DQLMTVLANV THLLIRANYN SAKMALYRLQ SVSLDIASPN AIDLAVAADV EHCECPQGYT
GTSCELCLSG YYRVDGILFG GICQPCECRG HAAECDVHGI CIACAHNTTG NHCERCLPGF
YGEPSRGTPG DCQPCACPLT IASNNFSPIC HLNDGDEVVC DQCAPGYSGA WCERCADGYY
GNPTVPGESC VPCDCSGNVD PSEAGHCDSV TGECLKCLGN TDGAHCERCA DGFYGDAVTA
KNCRACGCHA KGSYSAVCHL ETGLCDCKPN VTGQQCDQCL HGYYGLDSGH GCRPCNCSVA
GSVTDDCTDE GQCHCVPGVA GKRCDRCARG FYAYQDGSCT PCDCPHTRNT CDPETGECVC
PPHTQGVRCE ECEDGHWGYD VEVGCQACNC SLVGSTHHQC DVVTGRCQCK WKFGGRACDQ
CSLGYRDFPD CVPCDCDLRG TSGDACNLEQ GLCGCAEETG ACPCKENVSG PQCNECQEGS
FALRADNALG CSPCFCSGLS HLCSELEGYV RTPVTLGSDQ PLLRVVSQSN LRGTTEGVYY
QAPDFLLDAA TVRQHVYAEP FYWRLPRQFQ GAQLMAYGGK LKYSVAFYSL DGVGPSNFEP
QVLIKGGRTR KQVIYMDAPA PENGVRQEQE VAMREHFWKY FNSVSEKPVT REDFMSVLSN
IEYILIKASY GQGLQQSRIS DISMEVGRKA EKPHPEEEVA SLLENCVCPP GTVGFSCQDC
APGYHRGKLP AGSGRGPRPL VAPCVPCSCN NHSDTCDPDT GKCLNCGDNT AGDHCDVCAS
GYYGKVTGSS SDCALCVCPH SPPASFSPTC VLEGDHDFRC DACLLGYEGQ HCERCSLGYY
GNPQTLGGSC QKCDCNPHGS VHGDCDRTSG QCVCRLGASG LRCDECEPRH ILMETDCVSC
DDECVGVLLN DLDEIGDAIL SLNLTGIIPV PYGILSNLEN TTKYLQESLL RENMQKDLGR
IKLEGVAEET DNLQKKLTRM LASTQKVNRA TERIFKESRD LAIAIERLRM NITEIIEKTT
LNQTLDEDFL LLNSTLQSMQ QNGTSLLEIM QRRDFTQLHQ NATLELKAAE DLLSQIQENY
QKPLEELEVL KEATSHFLSK HNSELKAAEV LVREAEAKTQ ESNHLLFMVN ANLREFSDKK
LHVQEEQNLT SELIAQGQGL IDTAAAQTDA VQDALVHLEH HQDTLLLWSA KIRHHVDDLV
MHMSQRNALD LVYSAEDHAA EFQRLADVLD SGLENVRNVS LNATSAAYVH YNIQNLIEES
EELARDAHRT VTEMSLLSES LVSNGKAAVQ RSSRFLNEGD NLSRKLPVIA LELNELRNKT
NRFQENADEI TRQTNESVLI LRAIPEDTRN KGAKTKELAT SARQSAVSTL RDVAGLSQEL
LSTSASLSRV NTTLQETHQL LQDSTMATLL AGRKVKDVET QANLLFDRLK PLKMLEENLS
RNLSEIKLLI SQARKQAASI KVAVSADRDC IRAYQPQISS TNYNTLTLNV KTQEPDNLLF
YLGSSTSSDF LAVEMRRGEV AFLWDLGSGS ARLQFPDFPI DDSRWHSIHV ARFGNIGSLS
VKEMSSNQKP PAKTSKSPGT ANVLDVNNST LMFVGGLGGQ IKKSPAVKVT HFKGCLGEAF
LNGKSIGLWN YIEREGKCHG CFGSSQNEDP SFHFDGSGYS VVEKSLPATV TQIIMLFNTF
SPNGLLLYLG SYGIRDFLSI ELFHGRVKVT TDLGSGPLTL LTDRRYNNGT WYKIAFQRNR
KQGVLAVNDA YNTSNKETKQ GETPGASSDL NRLDKDPIYV GGLPRSRVVR RGVTAKSFVG
CIKNLEISRS TFDLLRNSYG VRKGCSLEPI RSVSFLKGGY IELPPKSLSP ESEWLVTFAT
KNSSGIILAA LGGDAEKQRD REESHVPFFS IMLIGGNIEV HVNPGDGTGL RKALLHAPTG
TCSDGQAHSI SLVRNRRIIT VQLDENNPVE MKLGPLVESR TINMSNLYVG GIPEGEGTSL
LTTRRSFHGC IKDLIFNLEL LDFNSAVGHE QVDLDTCWLS ERPKPAPDAE DSELLPEPRA
FPEQCVVDAA LEYVPGAHQF GLSQNSHFLL PFNQSAVRKR LSVELSIRTF ASSGLIYYMA
HQNQADYAVL QLHGGRLHFM FDLGKGRTKV SHPALLSDGK WHTVKTDYVK RKGFITVDGQ
ESPMVTVVGD GTTLDVEGLF YLGGLPSQYR ARKIGNITHS IPACIGDVTV NSKQLDKDSP
VSTFTVNRCY AAAQEGTFFD GSGYAALVKE GYKVQTDVNI TLEFRTSSQN GVLLGISTAK
VDAIGLELVD GKVLFHVNNG AGRITATYEP KTATALCDGK WHTLQANKSK HRITLIVDGN
AVGAESPHTR STSVDTNNPI YVGGYPAGVK QKCLSSQTSF RGCLRKLALI KRPQVQSVDF
SRAFERPGVF LHSCPGTES
//
