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Database: UniProt
Entry: A0A087XY66_POEFO
LinkDB: A0A087XY66_POEFO
Original site: A0A087XY66_POEFO 
ID   A0A087XY66_POEFO        Unreviewed;      3038 AA.
AC   A0A087XY66;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Laminin, alpha 1 {ECO:0000313|Ensembl:ENSPFOP00000010719.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000010719.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000010719.2}
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   EMBL; AYCK01017478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 48698.ENSPFOP00000010719; -.
DR   Ensembl; ENSPFOT00000010734.2; ENSPFOP00000010719.2; ENSPFOG00000009921.2.
DR   eggNOG; KOG1836; Eukaryota.
DR   GeneTree; ENSGT00940000157124; -.
DR   OMA; TVRQHVH; -.
DR   Proteomes; UP000028760; Unassembled WGS sequence.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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; 11.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
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:SF409; LAMININ SUBUNIT ALPHA-1; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 2.
DR   Pfam; PF00053; Laminin_EGF; 15.
DR   Pfam; PF00054; Laminin_G_1; 3.
DR   Pfam; PF02210; Laminin_G_2; 2.
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; 14.
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; 12.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 3.
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|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT   DOMAIN          1..249
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          377..429
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          430..477
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          487..687
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          721..766
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          767..824
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          825..877
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          918..964
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          965..1010
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1011..1056
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1137..1322
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1365..1413
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1414..1468
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1469..1515
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2080..2266
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2274..2450
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2457..2643
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2685..2853
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2858..3035
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   COILED          2020..2075
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        377..389
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        405..414
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        448..457
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        739..748
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        795..804
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        849..858
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        861..875
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        918..930
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        938..947
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        983..992
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1011..1023
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1013..1030
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1032..1041
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1384..1393
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1439..1448
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1469..1481
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1471..1488
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1490..1499
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2616..2643
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   3038 AA;  328527 MW;  E565B7BEA919097A CRC64;
     GLFPAIFNLA NNAEISSNAT CGDPEPEVYC KLVEHVPGRR IKNPHCPRCD ANSVLAKERH
     PIINAIDGTN QWWQSPSIKN GRQFHWITIT LDLNQIFQVA YIIIKAANSP RPGNWILERS
     LDGVTFDPWQ YYAISDSECL HRYNITPRFG PPTYRSDTEV ICTSYYSRLN PLEHGEIHTS
     LINGRPGADD LTPDLLNFTS ARYIRVRLQR IRTLNADLMT LSVHDPRDVD PIVTRRYYYS
     IKDISVGGMC ICYGHAQSCP LDPVTKKLKC VCEHNTCGEN CNECCPGYHQ LPWQPGTLSE
     GNTCEKCNCH NKASDCFYNQ TISDLGLSLN RHGVRRGGGV CIDCQQNTIG TNCESCRDGY
     YRPAEASPYS DLPCVECSCD LRGSRSSVCH KDDTEPGLSV GQCQCKDGFS GRHCDRCAFG
     FRDFPACARC ECNLAGSTNS DPCSSCTCKV NVLGVHCDQC KPGFYDLQQQ NPLGCTDCFC
     FGVSDICQSS DWSVTQVMHL TCAQVVLSDA VLQPSDPVQA ALGVHGNDLG IPSNASSTVA
     HKHRLVWGAP RHFLGNKLVS FGGQLVFSVV YDVAPDNRDQ TLTVLSDVIM QGNGRTLRLS
     PPLLLFLLPL AEQPVAMEIY PDRFVDNRTG GPVTRHDLLL VLTDLTRLYV RVHLNTSTEG
     PIRLGSVSLD VASSGSGSGV RAVAVETCEC PAGYSGTSCE SCLPGFYRVG AVLFGGYCMQ
     CECSSRSTHC DITGVCQGCS HNTTGPHCEL CLPGFYRDPT NGDCRLCPCP LTEPSNSFSP
     TCVVEPSGQV SCDRCQPGYA GSNCERCASG FYGNPQVVGG ACVSCECNSN VNMSEAGYCD
     AVTGECLRCL GNTAGKHCEA CRPGYYGDAV ITKDCKDCGC DVNGSSSSVC DITTGLNTLL
     LSQLGFFGLQ SGRGCLPCGC IQSGSVSESC DQDGRCHCTE GVAGDKCDRC SRGYYGYHSR
     NCTECICDHT GGNCDPDSGE CICPPNTEGD SCDRCETGYW GHDPSTGCKP CSCSAAGSSA
     SRCHLLSGQC PCRDGFSGRS CDRCAPGYYG YPACSACDCD LAGTNETYCN KTLGVCECGW
     TGECVCKASV SGRRCEECVS GWFALSDQNP NGCFDCFCSG LSKDCEEQGG LTRVPVGLGP
     VLSLVSLSSQ QSVVSGVYQQ GGDMLLDTRQ LNSSGLAGPL YWRLPHQAEG NQLMSYGGLL
     SYIITFYAED GSGLSNQEPQ VLMRGGILRK HTIFTDVVAP SNGIVTQHDI RLTEHTWKYF
     NSVSQRAVTR VDFMSILSKV QDVLIKASYG TGLQRRISNV TMEAAVRAES DSSQEKARLI
     ESCLCPLGYS GRSCQVCSAG FFRQPQSELP AQSLKTMTVR PCLPCRCNNH SATCDPETGD
     CQDCQHHTSG RQCEVCSPGY YGNVSGSISD CSPCACPLVV NSFSPSCVSA AGGFRCTSCL
     TGYEGRRCER CSPGYHGNPT VPGGLCLPCG CSGWGSLHQV CDDLTGHCQC KPGVRGQSCD
     QCGERHVLHQ EQCVSCIDGC SAVLLDDLDR LNDRILSVNL SAVAMAPYHQ LVLLENRTKD
     FKIRLTSRHE RSGVSELLLQ RVSSLQDEIQ VEIFYLVTLT WVPVVRSQEV FTPQQSNTSD
     LIGSVLQKGV GLLNQTNDGE LTEDGAVRLE EAEVRLQRIR GVNLTAAGSA VNQELSLSEA
     LLRLLQMDLM SRWTPGKDRL HALSNSLGVA MTTLQHARAP LGEAAERNSE TEKLLDAAGA
     LQRHLQVSPS SRQAARQNLG SALVAVHRLM EDGQTMQKDA VSLSAQLTNR SAVELLASQL
     DQLRPALRKH VEVLLVGLKT SSALENVHRA EGHAHQLQSH AHSLHRLVNG SQSPAPWALL
     DDDVIQRVGS AHQEAGSGLI AASLALHLTG QSEQTLAEEG GARLNVASRV LEESWQFNAT
     AEVLQANVSM VTTKLQLARD GMENCSRLLH HPIRELQQLP PGDRPSAAGS SRLAQLQAEQ
     AHLGLQGVLL RLQGLWLQLQ NSSSVVEKTH ITVRETSGLM GRAQATANEV QRRLEEAEHR
     TKQLLERLKP LSMLGETLSR NLSDIRELID QARRQAASIK VAVQADRNCV RSYRPPVQSS
     NFNTLSLVLK TSRPNNLLFY LGSNTTVDFL AVEMHHGKVS LLWNLGSGTT QLQFPETDIA
     NNRWTKINAT RFGAHAALSV HQLDSRSAPL PAVTSPSPGL SRVLDIDRNT VIHIGGMGAF
     TQVALRQVDR WLHSSSFQGC LGEASLNEQN IGLWSYVSRE GQCSGCFSSP QAEETSFYFD
     GSGFSMVQKS LKATSTSIVL LFKTLSPGGL LLYLASNNTR DFLSLELVEG HVRLAFDLGS
     GVLVQTSNRK YNTGVWFKVT LQRNKRKGYL SVMAADQSLE KEVLEAESPG TASDLNRYDL
     DPIYIGGFPS SRPIRRQVVS RAYVGCIKNM EIARSNFDLL KNAFGVRKGC VLKAVRSVSL
     LSGGFVQIAP PSFGQEAEFL FTFSSNNQSG VLLAAFSDDR VNRQVRPTQY FLSLHLVSGG
     VEAEVGDLGG ATRKVKVLKS GGGSFGDGSE HSVVMTVNRK SLSLQVDDVH LKSAPLMFGG
     FSRLTPSSLF IGGLPPEKES RLPIRLRVSS QRFRGCIHHL VVGGALVDLS VAVRYKGAEL
     NTCLLERSTA GAVLPDNPDI ESMPAGDWFV LKCVAEQEIS FLPSTAQFGS SSHSHMTFLI
     NPGAFRKIVS VRLSVRSRAL DGLMLLLSDA KQMDFVVLGL RGGRVRLSAD LGKGPASVLS
     ATVNDGHWHS VSAEVSRRSV SLTVDGSRPA TASIKGNHLD VDRTLFLGGL PASVNGRRIG
     VSSSLPGCLR SVSLNGTMLD LSKPFSQHDV TSCFTKDQTG SYFNGSGHAE FMHDGYKVGA
     DMAVSLEFRT SQSEGIFLGI SSAKVDAVGL EMVDGQVVFN VNNGAGRMAL RSTGPMLCDG
     RWHHLVARKT KHGLALSVDG TQYSAANPYP QSTSAETNNP VYLGGVPASV KQNCLSVRSG
     FRGCLRNLRL ARSHLNLPLH LSSAHFLSGV TPDSCPAS
//
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