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Database: UniProt
Entry: A0A3P9NHQ5_POERE
LinkDB: A0A3P9NHQ5_POERE
Original site: A0A3P9NHQ5_POERE 
ID   A0A3P9NHQ5_POERE        Unreviewed;      1411 AA.
AC   A0A3P9NHQ5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Multiple EGF like domains 6 {ECO:0000313|Ensembl:ENSPREP00000009077.1};
GN   Name=MEGF6 {ECO:0000313|Ensembl:ENSPREP00000009077.1};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000009077.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000009077.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000009077.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   Ensembl; ENSPRET00000009186.1; ENSPREP00000009077.1; ENSPREG00000006025.1.
DR   GeneTree; ENSGT00940000156971; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000006025; Expressed in caudal fin and 1 other cell type or tissue.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   Gene3D; 2.10.25.10; Laminin; 8.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 7.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR042635; MEGF10/SREC1/2-like.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   PANTHER; PTHR24043:SF8; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF14670; FXa_inhibition; 5.
DR   Pfam; PF00053; Laminin_EGF; 6.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 28.
DR   SMART; SM00179; EGF_CA; 5.
DR   SMART; SM00180; EGF_Lam; 20.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 16.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 9.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1411
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018048121"
FT   DOMAIN          56..96
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          308..348
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          444..479
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          834..869
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          877..912
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          920..955
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          968..998
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1093..1128
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1265..1300
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1343..1411
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   DISULFID        469..478
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        859..868
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        902..911
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        945..954
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        988..997
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1118..1127
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1290..1299
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1367..1374
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   1411 AA;  150843 MW;  92B618FF6EAFBAA6 CRC64;
     VMALAAGWWI FFLVLIEATA SLAANYPYVY YRRICHRPHC YYGYHGYNTG YLPAADIDEC
     QVHNGGCQHR CINTRGSYYC ECHPGSRLHV DGRTCLTVFS CAVRNGGCEH YCLQQSASHF
     RCRCKPNYVV AEDGKHCKLQ NPCADQNGGC MHECRVDGGK PFCDCKRGYL LAEDGKTCED
     IDECKTEETN CAHGCRNTLG SYACVCNTAY ELGSDGKQCY RIEMEIVNSC ESNNGGCSHH
     CQHSTSGPVC TCNHGYRLND DLKTCVDVDE CGEQSSCCEQ DCTNYPGGYE CYCSAGHRLN
     ADGCSCDDVD ECLAANGACD HTCQNTAGSF QCFCRRGFQL DQDRRSCICA VELSLIHPQL
     TLLRDYDQPL ERYDNYEDDD GELRAESSLA EKFVCLDDTF GSDCSLTCDD CTNGGICNIW
     KNGCDCPDGW TGIICNQTCP AGHFGKNCSF SCKCKNGASC DSVSGSCRCP PGVTGDLCQD
     GCPKGFYGKQ CNKKCNCANN GRCHRTYGAC LCEAGLYGRF CHLPCPKWTF GAGCSQECQC
     DQKKTKHCHR HHGTCICKPG YHGSTCCKTG TFGLGCEQKC ACPPGASCDH VTGACQRKCP
     AGRHGEKCEQ ECPEGMFGPG CIQPCNCTGA PCDKETGQCH CQAGTHGEHC ENFCDAGHWG
     AGCAETCDCR NGDGSCDAVT GRCSCEAGFT GPSCQQSMLL QYLLNFFTCF ICCHIAASNL
     CVLVRRIKEQ CPFHSCLLVF GLPSECPAGL FGLSCRRLCQ CENEAQCDHV SGACTCQVGW
     TGSFCEKPCP QGFYGLDCQE KCFCQNGGSC DHVSGVCSCP AGWIGTFSCL AGFYGPGCNR
     TCGCRNGGIC HPAGGQCSCM PGWTGPNCTE ECPAGLYGAD CQQVCLCQNG ATCNKTDGKC
     SCPAGWTGTA CELECTAGRF GADCQQRCEC ENGGVCDSQA GRCSCSAGWV GERCEKACEA
     GLYGAGCTER CRCAHGVSCH HMTGECRCPP GWRGKLCDKA CLPGTFGEGC MQRCSCAQET
     SCHHISGECG CPPGFTGNGC EQTCIPGLFG PNCNRVCQCS ETNQLCHPVS GSCYCAPGFH
     GSKCDQSCEE GRYGPDCQKE CRCENGGRCV PSTGSCECPA GFIGPSCNIT CPVGRYGVDC
     NRVAACGDGA QNDPVTGRCV CIPGRRGEDC GQSCPPGWFG GDCTQRCNCS NGGLCDSATG
     NCTCGLGWTG ERCDIECPVG RFGANCQLKC SCQNNGSCDK VTGTCRCGSG YYGHLCEHVC
     PPGFHGPLCQ LQCDCMNGAT CHPVLGHCIC PPGHHGARCH RVCELGRYGQ GCVGVCDCED
     GSPCDPVTGR CICPSGKTGA RCDIDCRGDR YGPDCAETCE CKNGAQCDRH NGRCLCVHSW
     IGLSCQEGTP LTNTHALGRQ QASQNQRMYP C
//
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