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Database: UniProt
Entry: U3KEF3_FICAL
LinkDB: U3KEF3_FICAL
Original site: U3KEF3_FICAL 
ID   U3KEF3_FICAL            Unreviewed;      1516 AA.
AC   U3KEF3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Zinc finger FYVE domain-containing protein {ECO:0000256|PIRNR:PIRNR037289};
GN   Name=ZFYVE16 {ECO:0000313|Ensembl:ENSFALP00000013407.1};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000013407.1, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000013407.1, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000013407.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037289}. Early
CC       endosome membrane {ECO:0000256|PIRNR:PIRNR037289}.
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DR   RefSeq; XP_005061340.1; XM_005061283.1.
DR   RefSeq; XP_005061341.1; XM_005061284.2.
DR   STRING; 59894.ENSFALP00000013407; -.
DR   Ensembl; ENSFALT00000013463.2; ENSFALP00000013407.1; ENSFALG00000012844.2.
DR   GeneID; 101812605; -.
DR   KEGG; fab:101812605; -.
DR   CTD; 9765; -.
DR   eggNOG; KOG1841; Eukaryota.
DR   GeneTree; ENSGT00940000154290; -.
DR   HOGENOM; CLU_004326_0_0_1; -.
DR   OMA; GIDKYVC; -.
DR   OrthoDB; 3061552at2759; -.
DR   Proteomes; UP000016665; Chromosome Z.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd15729; FYVE_endofin; 1.
DR   Gene3D; 3.30.500.40; -; 1.
DR   Gene3D; 3.30.1360.220; Domain of unknown function (DUF3480), N-terminal subdomain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR022557; SARA-like_C.
DR   InterPro; IPR035438; SARA/endofin.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46319; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46319:SF1; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 16; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF11979; SARA_C; 1.
DR   PIRSF; PIRSF037289; SARA/endofin; 1.
DR   SMART; SM01421; DUF3480; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR037289};
KW   Endosome {ECO:0000256|PIRNR:PIRNR037289};
KW   Membrane {ECO:0000256|PIRNR:PIRNR037289};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR037289};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          720..778
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          266..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..839
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          913..968
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1374..1393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        921..938
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        953..968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1374..1389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1516 AA;  163554 MW;  F1F82181A3048C12 CRC64;
     MDSYFKAAVC DLDKLLDEFE RNTDECECFR TPQNPYDSKL SSVLDCLEHA DPRAGQPEDP
     ARCPAPEQSS LCAPADTGDV LSYSPPREKG VAGPDLLSTV DSGPLSETQA LKLGRCSIPV
     CDLVSDTANL KHSVAAAEGP QKLQPDHLQC SQAGCGVSCV PVPACVTSPG CSGAASTKHS
     DGDSVLQDAG HLTAEQSNNL ALKSESYAAG AVLDLCDDQH RTEPVKCNEI LDHPEQTAAL
     DTECVTVAPQ SWSAHSPKDE KACEKLPFTP QDDSARSAAS TEVCGGNAIG KVDPNHESNA
     DSMPSDLPKR HLLHSSNAAS PGNGVLPGSS CQIGAEAELE KRGAEDNVDS EELNSRERVS
     SSEIVSSVSS SCMSAEDVQT SLSCLSLPVS MCGSLVATEE KVNPLPQNAV AEVISDTVAI
     HAGEPKAHLP GRESCESTSW REQEDLAEIS ESIAEKGSDG EKYSTENVTD DGDSQQIKGF
     ASAFLDLGAE PYSVGVDTFY DESMSSVMAD FTVEENVIKS DILISDAELD DFLYGQSLQS
     SVLKSSDSDG NLMEADADGG DLTDLNNLVF TEISEELVQT KLEEITSINS NLKASVPDNE
     VEAAAKVSMS HGQGVTESGS GALASDVCIK GARPKQLLDL SQGAAGQKQL NRTSEPEREN
     QESGSVTAEA PLSGISVNAG NNYDPGESSC EAGGNQTSES AESRRTPPAL SWKQPLWVPD
     SEAPNCMNCQ AKFTFTKRRH HCRACGKVFC GSCCKRKCKL QYMEKEARVC TGCYDDINKA
     QAFERMMSPT GPVPNSSVSS EHSSAVPPVE EGQVPAGASS PSPSALLPTS ALKQPGPEGL
     CPREQKRVWF ADGILPNGEV ADTAKLSSGA KRSQDCSPVT PELPQTPTAA NPEEDDLITD
     VNQKLKEEID KIPRMEELHP SVPSDSTQQA TPGQSEVTPG YKSGGEECSP AAAEESSPSS
     VEQSTQGVPV TASSYRALCG VENWVPREIS LLPDGDQLPP LLLALGERGK DILVEEHPFH
     QKVTLLLGEG GPNPLTFILN ANLLVNVKLI TYSSEKCWCF STNGLHGLGQ AEIVILLQRL
     PDEDVFPSEI FKLFLDIYKD AMKGRFIKNM ENITFTENFL SNKEHGGFLF VSPTFQKLDD
     QILPDKPFLY GILIHKLEIP WAKVFPIRLM LRLGAEYGAC PTPVVSVRHR KPLFGDIGHT
     IMNLLVDLRN YQYTLHTIDN LFVHVEMGRS CIKIPLRRYN EVMRVINSSN EYVISIGASF
     NTEADSHLVC VQNKQGLYHT QAISATGQPR KVTGASFVVF NGALKTSSGF LAKSSIVEDG
     LMVQITRETM ESLRQALRDK KDFKITCGKM DAGDVKEYVD ICWVENEEKT NQGILSPVDG
     KSMEGTQSEK APQYRDFERD GKVMKCTEVY YFVKDHELPG AVAHQFAKEI AIACSTALCP
     HLKTLKNNGM NKIGLRVSID SDMVEYLAGS GGYLLPQNYL NDLDSALIPV IHGGMSDPAA
     LPLKMELVFF IIEHLL
//
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