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Database: UniProt
Entry: A0A091PZE7_LEPDC
LinkDB: A0A091PZE7_LEPDC
Original site: A0A091PZE7_LEPDC 
ID   A0A091PZE7_LEPDC        Unreviewed;      2139 AA.
AC   A0A091PZE7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   SubName: Full=Laminin subunit alpha-1 {ECO:0000313|EMBL:KFQ13322.1};
DE   Flags: Fragment;
GN   ORFNames=N330_08004 {ECO:0000313|EMBL:KFQ13322.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae;
OC   Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ13322.1};
RN   [1] {ECO:0000313|EMBL:KFQ13322.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ13322.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   EMBL; KK682826; KFQ13322.1; -; Genomic_DNA.
DR   PhylomeDB; A0A091PZE7; -.
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   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   Pfam; PF00052; Laminin_B; 2.
DR   Pfam; PF00053; Laminin_EGF; 17.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 11.
DR   SMART; SM00180; EGF_Lam; 17.
DR   SMART; SM00281; LamB; 2.
DR   SMART; SM00136; LamNT; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 5.
DR   PROSITE; PS50027; EGF_LAM_2; 15.
DR   PROSITE; PS51115; LAMININ_IVA; 2.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00460,
KW   ECO:0000256|SAAS:SAAS00966286};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Repeat {ECO:0000256|SAAS:SAAS00580781}.
FT   DOMAIN        1    257       Laminin N-terminal. {ECO:0000259|PROSITE:
FT                                PS51117}.
FT   DOMAIN      258    314       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      315    384       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      385    441       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      442    490       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      511    696       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN      730    778       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      779    836       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      837    889       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      890    938       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      939    985       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN      986   1031       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1032   1077       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1078   1137       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1165   1349       Laminin IV type A. {ECO:0000259|PROSITE:
FT                                PS51115}.
FT   DOMAIN     1391   1439       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1440   1496       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   DOMAIN     1497   1543       Laminin EGF-like. {ECO:0000259|PROSITE:
FT                                PS50027}.
FT   COILED     1746   1773       {ECO:0000256|SAM:Coils}.
FT   COILED     2057   2077       {ECO:0000256|SAM:Coils}.
FT   COILED     2081   2105       {ECO:0000256|SAM:Coils}.
FT   DISULFID    280    289       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    352    361       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    385    397       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    417    426       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    461    470       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    748    757       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    807    816       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    861    870       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    873    887       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    890    902       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    892    909       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    911    920       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    939    951       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID    959    968       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1004   1013       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1032   1044       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1034   1051       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1053   1062       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1078   1090       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1108   1117       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1410   1419       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1467   1476       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1497   1509       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1499   1516       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   DISULFID   1518   1527       {ECO:0000256|PROSITE-ProRule:PRU00460}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFQ13322.1}.
FT   NON_TER    2139   2139       {ECO:0000313|EMBL:KFQ13322.1}.
SQ   SEQUENCE   2139 AA;  235070 MW;  9FD200FD83BED284 CRC64;
     QGLFPAILNL ASNAHISTNA TCGEKGPEMF CKLVEHVPGR PLRNAQCRVC DHHSANPKGK
     FHMVGEQHPI SSAIDGTNNW WQSPSIQNGR QYHWVTITLD LRQVFQVAYV IIKAANAPRP
     GNWILERSLD GTEFRPWQYY AISDTECLTR YNITPRIGPP TYKRDDEVIC TSYYSRLVPL
     EHGEIHTSLI NGRPSADDPS QKLLEFTSAR YIRLRLQRIR TLNADLMTLS HNDPKELDPI
     VTRRYYYSIK DISVGGMCIC YGHARSCPLD EITKKLQCQC EHNTCGESCN KCCPGYHQKP
     WRPGTISAGN KCEKCNCHNK AEDCYYNQSI ADQKKSMDVH GQYIGGGVCL NCTQHTTGIN
     CEMCADGYFR PQKVSPYEDH PCYPCGCDPF GSLSSDCVKD EHHSDSQRGT WPGQCRCREG
     YAGEKCDRCA FGYRGYPNCL RCNCSLIGSI NEDPCTEPCL CKENVEGENC DLCKPGFYNL
     QERNPQGCTE CFCFGVSDVC DSLTWPISQI SDMTGWLVTD LYNARSMQPQ RSQFDGPHQI
     SINNTEAVKV LKHAYYWSAP EIYLGNKLTA FGGDLKYTVS YDIPMESMDS DIVSSVDVII
     QGNGQILGTR AAGLSLQPYE EYSNAVRFVS ENFIDFNTKK AIDRERLMTV LVNVTHLLIR
     ANYNIAKKAV YRLDSVTLDT ASANVIDLSS APDVEFCECP QGYTGISCES CLPGYYRVDG
     ILFGGICQPC KCNGHATECD IHGVCFACQH NTTGPFCDQC LPGFYGSPSQ GTSEDCQPCA
     CPLSSAANNF SPTCQLSEGG QIVCDKCLPG YTGSQCERCA NGYYGNPLMP GQSCAPCECN
     GNVNPQEDGH CDTFTGQCLK CLGNTAGHHC ERCADGYYGD AVTEKSCHAC ACHVNGSLSS
     TCHHETGFCH CKSNVIGERC DKCLNGYYGL LTGLGCVPCN CSQFGSVSEA CDHQGQCHCV
     PGVAGEKCDR CAHGFHAFQD GGCTPCDCAH TQNNCNPDSG QCICPPHTRG PKCELCEENH
     WGLSPKLGCK DCNCSNTGSA NLQCDVLTGQ CQCKVEFGGQ DCSRCALGYR DYPDCVACDC
     DLSGTKAEMC DDTEGLCGCE EETGICTCKE NVFGLQCSEC KPGTFALSAN NALGCTPCFC
     FGMSMFCSEL EDHVRIPITL TPDQSILRVV AQSNLTGTVE GVFSQFPDVL LDAAVVRKYL
     NTETFYWRLP EQFQGDQLMA YAGKLRYTVA FYALDGFGTS NFEPQILMKG GHTSKLVIYV
     DIPAPENGVR SDKEVEMKED SWKYFNSVSD KPVLRSDFMS VLSNVEYILI KAAYGQGLQQ
     SRIANISMET AVKFEEMHLG RAKAHLVEQC RCPAGYAGLS CQSCAPGYYR GKHTELSVKE
     PHALMTPCVP CQCNNHSETC DPETGKCLNC RDNTVGDYCS ACAPGYYGKV LGSVNDCSLC
     ACPRANPVSF SPTCVLKGVQ DYQCDACLPG YEGQYCERCS LGYYGEPQLP GGSCHPCRCN
     PSGSVHVNCD RATGQCLCKQ GVTGQLCEEC EPRHLLVEDE CVSCDDNCTG VLLNSLDHLN
     KAMLSMNLTG VARVPYGILA ELENATKHLK GSIVPREDPT YSLTTAKETL LSLSGGIDQL
     HEESSRFLKK AWKLNTVTQE TRNKSQELTG FIDTVHATIK VLAEVAMSLN ETLGLHLPLS
     NATSQSLQDD ISALLDALRK KDFAQQHHNA SSVLKAAENL LIQVQKEYLK PQEELAELKK
     DASQLLSKHN SRLQDVQDLA NEALANVNET NRLFPLISSN LAELNDKKLN IKEGEEVSTA
     LIKEGEVLVN AAAALAQDVK NSTSNLEVHQ DGLVLWSTKL RHHVDELVMQ MSVRGVLDLV
     YRAEEHATQF QRLADALESG LSKVRNVTLN TTAAVYAHSS VKSVIERTES LADDASRVVN
     GPLYLPEESL GVLGKETLLL SSKFQNEAKN VKKKSDDLLF GLNGLNKRVE KIQKSTNKIV
     NQLNDSLLTL RALPNDARKY MFEVKDLAMS ANTSAVVGLS HFGDFNQKLL NTSSTLSRVN
     DTLRKTSELI TDSSKAAVTA EKQVKEVEAQ ASLLLDRLKP LKMLEENLSR NLSEIKELIS
     QARKQAASIK VAVSADRDCI RAYQPQISST NYNTLTLNV
//
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