ID G1LM02_AILME Unreviewed; 3079 AA.
AC G1LM02;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Laminin subunit alpha 1 {ECO:0000313|Ensembl:ENSAMEP00000007979.2};
GN Name=LAMA1 {ECO:0000313|Ensembl:ENSAMEP00000007979.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000007979.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000007979.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000007979.2}
RP IDENTIFICATION.
RG Ensembl;
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 STRING; 9646.ENSAMEP00000007979; -.
DR Ensembl; ENSAMET00000008310.2; ENSAMEP00000007979.2; ENSAMEG00000007475.2.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000157124; -.
DR HOGENOM; CLU_000301_0_0_1; -.
DR InParanoid; G1LM02; -.
DR TreeFam; TF335359; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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; 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; 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; 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; 16.
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; 14.
DR SMART; SM00180; EGF_Lam; 16.
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 SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01248; EGF_LAM_1; 7.
DR PROSITE; PS50027; EGF_LAM_2; 12.
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:UP000008912};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..3079
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030170939"
FT DOMAIN 23..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 795..852
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 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 COILED 1967..1994
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 823..832
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; 336315 MW; 1C84B76B045EE958 CRC64;
MRGGGGAGFA LLASLLWVAA RCQQKGLFPA ILNLASNAHI STNATCGEQG PEMSCKLVEH
VPGRPVRNAQ CRICDANSAN PKERHPISNA IDGTNNWWQS PSIQNGREYH WVTITLDLRQ
VFQVAYVIIK AANAPRPGNW ILERSLDGTT FSPWQYYAVS DTECLTRYNI TPRRGPPTYR
ADDEVICTSY YSRLVPLEHG IHTSLINGRP SADDLSPKLL EFTSARYIRL RLQRIRTLHA
DLMTLSHRDP RDLDPIVTRR YYYSIKDISV GGMCICYGHA SSCPWDETTK KLQCQCEHNT
CGESCSRCCP GYHQQPWRPG TISAGNTCEK CNCHNKAQDC YYDENVANQR RSLNVAGQFR
GGGVCINCLQ NTMGINCETC IDGYYRPYKV SPYEDNPCRP CDCDPFGSLS SVCIKDELQS
GLHKGKQPGQ CPCKEGYAGE KCDRCQFGYK AYPACVRCEC SRAGSVNEDP CSEPCLCKEN
VKGDNCDLCK PGFYNLKERN PEGCSECFCF GVSDVCDSLS WSISQVKDMS GWLVTDLISP
SKIPSQQDAL GGRHQISINN TSVMRRLTSK YYWSAPEAYL GNKLTAFGGF LKYTVSYDIP
VETVDGDLMS HADVIIKGNG LTLSTQAEGL SLQPYEEYLN VVRLVPENFR DFNNKREVDR
DQLMTVLANV THLLIRANYN SAKMALYRLD SVSLDTASPN VIDLALATEV EHCECPQGYA
GISCESCLPG YYRVDGILFG GICQPCECHG HAAECDIHGV CFACEHNTTG DHCEQCAPGF
YGLPSRGTPG DCQRCACPLS TASNNFSPTC HLEDGDEVVC DQCAPGYSGA WCERCADGYY
GNPTVPGESC VPCDCSGNVD PFEEGHCDSV TGECLKCIGN TDGAHCERCA DGFYGDAVTA
KNCSACECHG KGSLSDVCHL ETGLCDCKPH VTGRQCDQCL PGYYGLDAGL GCLPCNCSTS
GSVSDDCTQE GRCHCVPGVA GEKCDRCARG FYAYEDGGCT PCDCAHTQHT CHPESGECIC
PPHTRGAACD ECEDGYWGHD LELGCQACNC SGVGSARPGC DALTGHCQCK PGFGGPNCHQ
CSLGYRGFPD CVACDCDLRG TSADTCDEER GLCSCAEETG SCSCKENVFG LRCSKCRAGA
YGLRADDPLG CAPCFCFGLS QACSELQGYV RTPVTLGGGQ PLLRVVSQSN LQGTTEGVYY
QAPDVLLDAV TVRRHVHAEP FYWRLPDQFQ GDQLLAYGGS LKYSVAFYSS DGFGAFNLEP
QVLLKGGRTR KQVIYVDVPA PENGVRQEQE VGMKENFWKY FNSVSEKPVT RSDFMSVLSN
IEYILIKASY GQGLQQSRIS NISMEVGRKA GELHPGQKAA SLLEKCVCPP GTAGFSCQDC
APGYHRGRLP PDGSQGPRPL LAPCVPCICN NHSDACDPET GKCLDCRHST AGDHCDVCAP
GYYGKVTGSP SDCSPCACPR SHPASFSPTC VLEGDADFRC DACILGYEGQ YCERCSSGYH
GNPRAPGGTC QRCDCSPRGS VHGDCDRRSG QCVCRPGATG LRCEECEPRH ILLESDCVSC
DDECVGVLLN DLGNIDDTIL SVNLTGIIPV PHGILSTLEN TTKSLREALL KENPQKELAK
DQLEGVAEQT DNLLRELARV LTSSQNVTRV TEGILNKSQD LMTFTEKLQI NIQEIIEKAT
TLNQTLDEDF QLPSSTLQNM QRNITSLLEI IQKRHFKQLH QNAIQELKAA EDLLSQIQKN
YRKPQKELEV LKAAASSLLS KHSSELRAAG DLARGAEAEA RESARLLRIA HANLREFHEK
KLRVQEEQNL TSTLIARGRR LLAAVTARAE ATQNVLAQLE RHRDELLLWT AKIRHHVDDL
VMQMSQRRAL DLVYRAEDHA AELQRLAGAL DSGLGDVKHV SLNATSASHV HSNIRSLIEE
SEKAAKDALE TVTTASLFSE SLVSNGKVAL QRSSRFLKEG NSLSRKYQDI TLELSELKNA
ANRVQESADT ITRRANESRL ILRAIPGGVR GKGTKVKELA TAANQSAAST LKDVVGLSQK
LLNTSADLSR VNATLQETNK LLQYSSMTTL LAGRRMKDAE AQASLLFDRL EPLKILEENL
NRNLSEIKLL ISQARKQAAS IKVAVSADRD CIRAYQPPTS STNYNTLTLN VKTSEPDNLL
FYLGSSASSD FLAVEMRRGK VAFLWDMGSG STRLEFPDFP IDDNKWHSIY VTRFGNIGSL
SVKEMSATQK PPTKTSKSPG TANVLDINNS TLMFVGGLGG QIKKSPAVKV THFKGCMGEA
FLNGQSIGLW NYIEREGKCH GCFGSPQNED SSFHFDGSGY SVVERTLRAA GTHIIMLFST
FSPNGLLLYL ASNGTKDFLS IELVRGRVRV TVDLGSGPLA LITDRRYNNG TWYKIAFQRN
RKQGILAVID AYNTSYRETK QGETPGASSD LNRLDKDPIY VGGLPRSRVV RKGVTSKSYV
GCIKNLEISR STFDLLRNSY GVRKGCILQP IRSVSFLKGG YVELSPKSLS PESELLATFA
TKNSSGIILA ALGRQGEKQG QLQAHGPFFS IMLIEGHIEV HVNSGDGTSL RRALLRAPKG
TYGDGQEHSI SLIRTGRVIT VQMDEMNPVE MKLGPSAESR AINVSKLYLG GIPDGEGTSV
LKMRSSFHGC IKNLIFNMEH LDFTSAAGNE QVDLDTCLLS ERPQLALHGE DSELPPESQP
LPEQCAVDRA PEYIPHAHQF GLTQSSHFVL PFNQLAVRKR LSVQLRIRTF ASSGLIYHMA
HQNQVDYATL QLHGGRLHFL FDLGKGRTKV THPALISDGR WHTVKTEHFK RKGFMTVDGQ
ESPTVTTVGD GTMLDVEGKL YLGGLPSEYR ARNIGNITHS VPACIGEVTV NGKQLDEDNP
VSASAVTRCY AVAQEGTFFD GSGYAALVKE GYKVHSDVNI TLEFRTTTEN GVLLGISSAK
VDAIGLEIVN GKILFHVNNG AGRITATYKP KASTTLCDGK WHTLQAQKSK HRLVLTVDGN
AVRAESPHTQ STSADTSNPI YVGGYPADVK QNCLSSQTSF RGCLRKLTLI KGPQIQSYDF
SRAFDLQGVF PHSCPGSEP
//
