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Database: UniProt
Entry: A0A2U4BJJ0_TURTR
LinkDB: A0A2U4BJJ0_TURTR
Original site: A0A2U4BJJ0_TURTR 
ID   A0A2U4BJJ0_TURTR        Unreviewed;      1364 AA.
AC   A0A2U4BJJ0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Zinc finger FYVE domain-containing protein {ECO:0000256|PIRNR:PIRNR037289};
GN   Name=ZFYVE9 {ECO:0000313|RefSeq:XP_019793369.1,
GN   ECO:0000313|RefSeq:XP_019793370.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019793370.1};
RN   [1] {ECO:0000313|RefSeq:XP_019793369.1, ECO:0000313|RefSeq:XP_019793370.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019793369.1,
RC   ECO:0000313|RefSeq:XP_019793370.1};
RG   RefSeq;
RL   Submitted (NOV-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_019793369.1; XM_019937810.2.
DR   RefSeq; XP_019793370.1; XM_019937811.2.
DR   GeneID; 101337865; -.
DR   OrthoDB; 3061552at2759; -.
DR   Proteomes; UP000245320; Chromosome 1.
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:SF2; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 9; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF11979; SARA_C; 1.
DR   PIRSF; PIRSF037289; SARA/endofin; 3.
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:UP000245320};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          697..756
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          199..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1364 AA;  150012 MW;  19201569931A0047 CRC64;
     MENYFQAEAY NLDKVLDEFE QNEDETVSPI LLDTRWNKIL DPPSPRLSFN PALASVNEPT
     VSESQPRLKV FSLAHSAPLN TEGEDHCANG QDCSLNPETN TMWIDENAVA EDQLIKRNCN
     QDDQCGTVEV GEKKCGNLPC LPDEKSVLVV AVMHNCDKRT LQSDLQDCNN YNSQSLMDAF
     SCSLDNENRQ TDQFSLSVNG STEKDMNSEK QMDPLSRPNA EGDSVKYICT ASSDNLANVC
     TPSQLQDDEN IDRDPTMSVI TSLTPDSVIS SQGTDEGPAV KQEDSTPDEV LTGKTSSPRT
     DLGSPNSFSH LSEGILMKKE PAEERTTEES IQSGLPLLLK ADMPNGSGRD DNGEQFSDCL
     VPGEVRADEN EGCKHEEILG TTELLNMTEH FSESQEMINW KLTKPNKMND SQVNKENEKF
     LHMNQPEDTY DDSGGECDRM AEAGLDLKQT CMNESEGCDF STVMDTPAAN SLSNCCDSYG
     MQSPVVCFVP KTLPSKEDSV TEEKEIEESK SECYSNIYEQ RGNEATEGSG LLLNSTGDLM
     KKNYLHNFCS QVPSVLGQSS PKIVANLQSI SVPFGGARPK QPSNLKLQIP KPLSDHLQND
     LPANNGNNIK NKNDVLGKAK LGENSATNVC NASLGNISIA DTNGEHLESY ESGISSRQCV
     ALPPESPDND LRAGQFGISA RKPFTTLGEV APVWVPDSQA PNCMKCEARF TFTKRRHHCR
     ACGKVFCASC CSLKCKLLYM DRKEARVCVI CHSVLMNVAQ PREQRRVWFA DGILPNGEVA
     DAAKLTMNGT SSAGTLAVSH DPVKPVTTSP LSAETDISLF SGSITQVGSP VGSAMNLIPE
     DGLPPILIST GVKGDYAVEE KPSQISVMQQ LEDGGPDPLV FVLNANLLSM VKIVNYVNRK
     CWCFTTKGMH AVGQSEIVIL LQCLPDEKCL PKDIFNHFVQ LYRDALAGNV VGNLGHSFFS
     QSFLGSKEHG GFLYVTSTYQ SLQDLVLPTP PYLFGILIQK WETPWAKVFP IRLMLRLGAE
     YRLYPCPLFS VRFRKPLFGE TGHTIMNLLA DFRNYQYTLP VVQGLVVDME VRKTSIKIPS
     NRYNEMMKAM NKSNEHVLAG GACFNEKADS HLVCVQNDDG NYQTQAISIH NQPRKVTGAS
     FFVFSGALKS SSGYLAKSSI VEDGVMVQIT AENMDALRQA LREMKDFTVT CGKADAEDPQ
     EHIHIQWVDD DKNVNKGVIS PIDGKSMESI TSVKIFHGSE YKANGKVIRW TEVFFLENDD
     QHSCLSDPAD HSRLTEHVAK AFCLALCPHL KLLKEDGMTK LGLRVTLDSD QVGYQAGSNG
     QPLPSQYMND LDSALVPVIH GGACQLSEGP IVMELIFYIL ENIA
//
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