ID A0A2Y9LC60_DELLE Unreviewed; 3081 AA.
AC A0A2Y9LC60;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Laminin subunit alpha-1 isoform X1 {ECO:0000313|RefSeq:XP_022407245.1};
GN Name=LAMA1 {ECO:0000313|RefSeq:XP_022407245.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022407245.1};
RN [1] {ECO:0000313|RefSeq:XP_022407245.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022407245.1};
RG RefSeq;
RL Submitted (NOV-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_022407245.1; XM_022551537.2.
DR STRING; 9749.A0A2Y9LC60; -.
DR KEGG; dle:111163079; -.
DR InParanoid; A0A2Y9LC60; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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 CDD; cd00055; EGF_Lam; 15.
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; 15.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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; 11.
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; 13.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01248; EGF_LAM_1; 9.
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:UP000248483};
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..3081
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016063177"
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 1181..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 2122..2302
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2310..2486
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2491..2677
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2719..2891
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 2896..3076
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT COILED 1616..1643
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1734..1786
FT /evidence="ECO:0000256|SAM:Coils"
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 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 3081 AA; 337123 MW; 844A39290636A8ED CRC64;
MRGGGAGLAL LASLLWVAVQ GQQRGLFPAI LNLASNAHIS TNATCGEKGP ETYCKLVEHV
PRRAMRNAQC RLCDGSSANP KERHPISNAI DGTNNWWQSP SIQNGREYHW VTITLDLRQV
FQVAYVIIKA ANAPRPGNWI LEHSLDGMEF SPWQYYAVSD TECLTHYNIT PRRGPPTYRA
DDEVICTSYY SRLVPLEHGE IHTSLINGRP SSDDLSPKLL EFTSARYIRL RLQRIRTLNA
DLMTLSHRDP KDLDPIVTRR YYYSIKDISV GGMCICYGHA SSCPWDETIK KFQCQCEHNT
CGDSCNRCCP GYRQQPWRPG TVSSGNTCEE CNCHNKAKDC YYDENVANQK RSLNTAGQFR
GGGVCIDCLQ KTMGINCETC VDGYYRPHRV SPYDDNPCHP CDCDPLGSLS SVCIKNDLHS
DLHRGKWPGQ CPCKEGYAGE KCDRCQFGYK GYPACVPCDC NPAGSVNEEP CSEACLCKEN
VEGKHCDRCK PGFYNLEERN PQGCSECFCF GVSDVCDSLS WPISQVKDMS GWLVTDLVSS
SQLRSQQDTL GGRHQISINS SAVVQRLTSQ YYWSAPEAYL GNKLTAFGGF LKYTVSYEVP
VETADGDPMS HADVIIKGNG LTLRTQAEGL LLQPYEEHLN VVRLVPEHFR DFHSRREVDR
DQLMTVLANV THLLIRANYN SAKMALYRLD SVSLDTASPN VIDLSLATEV EHCECPQGYA
GISCESCLPG YYRVDGILFG GICQPCECHG HAAECDVHGV CFACQHNTTG DRCERCLPGF
YGLPSRGTPG DCQPCACPLS TASNNFSPTC HLNDGDEVFC DQCAPGYAGD WCERCADGYF
GNPTVPGDSC VPCNCSGNVD PLEARSCDSV TGECLRCLGN TDGPRCERCA YGFYGDAVTA
KNCRACECHG QGSLSAACHP ETGLCDCKPH VTGQQCNQCL HGYYGLDTGL GCLPCNCSAS
GSLSDDCTEE GQCRCVPGVA GERCDRCAHG FHAYQDGGCT PCDCAHTQNT CDPESGECVC
PPHTRGAACE GCADGHWGHD PELGCQACNC SSAGSASHHC DVLTGHCQCK PAFGGQTCHQ
CSLGYRDFPD CVACDCDLRG TLADTCGQEQ GLCSCAPETG TCSCKENVIG PQCSECQAGT
FALDEADPRG CTPCFCFGLS QLCSEAEGYV RMPVMLGSDQ PLLRVVSQSN LKGTTEGVYY
QAPDVLLDAV TVRRHVHTEP FYWRLPGQFQ GDQLMAYGSK LRYSVAFYSS SGIGTSNLEP
QVLIKGGRTR KQVIYVDAPA PKNGLRQEQE VGMKENFWKY FNSVSEEPVT RSDFMSVLSN
IEYILIKASY GQGLQQSRIS NISMEVGRKA EESHSRREVA SLLEKCLCPP GTAGFSCQDC
APGYHRGKLP EGDGRRPRPL LAPCVPCNCN KHSNTCDPET GKCLNCSHNT AGDHCDVCAP
GYYGKVTGSA SDCSLCTCPH GLPASFSPTC VLEGDHDFRC DACFPGYEGQ YCERCSSGYH
GNPQMPGGTC QRCGCSPHGS VHSDCDRGSG QCVCRPGATG LRCEDCEPRH ILVESDCVSC
DDECGGVLLN DMDHVGDAIV SVNLSGIIPV PYGILSNLEN TTKYLRDSLL KENIQKELAK
IQLEGVSEQT EDLQRKLDRV LTRSQHVTRA TKRILDKSRD LLTFTEKLQA DIQEIIERAA
TVNQTLDEDV QLPSSTLQNM QKNITSLLEI IQKRNFLQLH QNATLGLKAA EDLLSQIQKN
YQKPQEELEV LKEAASSLLS RHNSKVQATE ELLREAERKT QESSRLLFIV RANLREFNDK
KLRVQEEQNL TSVLIAEGRG LLDAATAPAN ASGKALAQLE HHRDELLLWT AKIRHHVDDL
VMQMSKRRAL DLVYRVEDHA TELQRLAGAL DSGLGNVSHV SLNATSATHV HSNIRSLIEE
SEKLVKDTLR TERKASVASE SLVSNGKAAL QRSAEFLKEG NSLSRKHGGI ALELSELKNT
AKRFQENADK ITKQTNESLL ILGAIPEGVR DKGTKIKELA TSANQSAMST LKNVVGLGQK
LLNTSTDLSR VNATLRETEE LLRDSSVTTL LAGRKVKDVE TQANLLFDRL KPLKMLEENL
SRNLSEIKLL ISQARKQAAS IKVAVSADRD CIRAYQPQIS STNYNSLTLN VKTSEPDNLL
FYLGSSISAD FLAVEMRRGK VAFLWDLGSG STRLEFPDFP VDDSKWHSIY VTRFGNIGSV
SVKEMSASQK PPPRTSKSPG TANVLDVNNS TLMFVGGLGG QIKKSPAVKV TYFKGCMGEA
FLNGQSIGLW NYIEREGKCH GCFGSPQNED ASFHFDGSGY SVVEKMLRAT VTQIIMLFST
FSPNGLLLYL ASNGTKDFLS IDLVDGRVRV TVDLGSGPLA LTTDRRYNNG TWYKIAFQRN
RKQGLLAVID AYNTSYKETK QGETPGASSD LNRLDKDPIY VGGLPRSRVV RRGVTSKSYV
GCIKNLEISR STFDLLRNSY GVRKGCILEP VRSVSFLRGG YVELPPKSLS PDSELLATFA
TRNSSGIILA ALGQHGEKQG HRQAHKPFFS IMLIEGHIEV HVNPGDGTSL RRALLHAPTG
TYGDGQEHSI SLIRTGRIIT VQLDETAPVE MKLGPSAESR TISVSNLYIG GVPEGEGTPM
LKMRSSFHGC IQNLIFNMEL LDFTSATGYE HVDLDSCLLS KQPKLALHGE DGELPPEPQP
LPSPELCVMD RAPEYVPNAH QFGLAGGSHL VLPFNQLAVR KRLLVQLSIR TFASSGLVYY
MAHQNQVDYA TLQLHGGRLH FMFDLGKGRT KVSHPALLSD GQWHTVKTEY FKRKGFMTVD
GQESPMVTTA GDATTLDVEG KLYLGGLPSE YRARNIGNIT HSIPACIGEV TVNSKQLDED
SPVSAFAVNR CYAAAQEGTF FEGSGYAALV KEGYKVRSDV NITLEFRTSS ENGVLLGISS
AKVDAIGLEI VNGKLLFHVN NGAGRITATY EPSAPNTLCD GKWHTLQANK SKHRVVLIVD
GNAVRAESLH TQSTSADTNN PIYVGGYPAD VKQNCLSSQT SFRGCLRKLT LIKGPQVQSY
DFSTAFDLQG VFPHSCPGTE S
//
