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Database: UniProt
Entry: A0A2Y9DBX7_TRIMA
LinkDB: A0A2Y9DBX7_TRIMA
Original site: A0A2Y9DBX7_TRIMA 
ID   A0A2Y9DBX7_TRIMA        Unreviewed;      1423 AA.
AC   A0A2Y9DBX7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Zinc finger FYVE domain-containing protein {ECO:0000256|PIRNR:PIRNR037289};
GN   Name=LOC101358561 {ECO:0000313|RefSeq:XP_004371789.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004371789.1};
RN   [1] {ECO:0000313|RefSeq:XP_004371789.1}
RP   IDENTIFICATION.
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_004371789.1; XM_004371732.1.
DR   STRING; 127582.A0A2Y9DBX7; -.
DR   GeneID; 101358561; -.
DR   KEGG; tmu:101358561; -.
DR   InParanoid; A0A2Y9DBX7; -.
DR   OrthoDB; 3061552at2759; -.
DR   Proteomes; UP000248480; Unplaced.
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; 4.10.720.10; Smad anchor for receptor activation, Smad-binding domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR022557; SARA-like_C.
DR   InterPro; IPR024608; SARA-like_SBD.
DR   InterPro; IPR035438; SARA/endofin.
DR   InterPro; IPR037145; SARA_Smad-bd_sf.
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; PF11409; SARA; 1.
DR   Pfam; PF11979; SARA_C; 1.
DR   PIRSF; PIRSF037289; SARA/endofin; 2.
DR   SMART; SM01421; DUF3480; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM01422; SARA; 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:UP000248480};
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          193..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1423 AA;  156008 MW;  1868892D7847F6E7 CRC64;
     MENYFQAEAY NLDKVLDEFE QNEDETVSPA LLDTKWNKIL DPPSHLLPFN PALASVNEPA
     VSNESQPQLK VFSLAHSAPL PTEGEDCCAN GQDNSLNAEI ATMWIDENAV AEDKLIKKNC
     NRDDQCSAVE GGEKKCGNLA CLPDENVLVV AVMHNCDKRT LQSDLQDCNN YNNQSLVDAF
     SCSLENESRQ TDQFSFSING STEKDTNSEK QMDPLTRPNK EGTSVHRLCT TSSDSLASVF
     SPSQLKNDEN IARDPSMSTI TSLTIDSVVL SQGIDESPAV KKQENCTPDE DLTGKTNSSR
     TDRGIPNSFS HSSEGILMKK ESTEERTMEE FLQSGLPLLL NPDMPNGSGR DDSCEQFSDC
     LVPSNVRVDE NEGYGHEVLD TREFLHMTEH FSETQEEMTN WKLTKLNEMS NNQVNEEDEK
     CLPVSQPEDT CDNGEESDGI AEAGLDLKRT YMNESEGCDF STVMDTPAAN SLSHGCDSCG
     MQSPVVAFVP KTLPSKEDSV TEEKEIEESK LECYSNIYEQ RGNEATEGSG LLLNSTGDLM
     EKNYLHNVCS QVPSVLGQSS PKIVGNVQSI SVPFGGARPK QPSNLKLQIP KPLSDHLQND
     VPANSGNNTK NKNDILGKAK LGENSATNVC NASLGNVSVA DTNGEHLESY EAGISSRPCL
     ALAPDSPDND LRAGQFGISA RKPFTTLGEV APVWVPDSQA PNCMKCEARF TFTKRRHHCR
     ACGKVFCASC CSLKCKLLYM DRKEARVCVI CHSVLMNAQA WENMMSASSQ SPNPNNPAEY
     CSTIPPLQQA QASGALSSPP PTVMVPVGVL KHPGAEVAQP REQRRVWFAD GILPNGEVAD
     AAKLTMNGTS SAGTLAVSHD PVKTVTTSPL PAETDISLFS GSITQVGSPV GSAMNLIPED
     GLPPILISTG VKGDYAVEER PSQISVMQQL EDGGPDPLVF VLNANLLSMV KIVNYVNRKC
     WCFTTKGMHA VGQSEIVILL QCLPDEKCLP KDIFNHFVQL YRDALAGNVV SNLGHSFFSQ
     SFLGSKEHGG FLYVISTYQS LQDLVLPTPP YLFGILIQKW ETPWAKVFPI RLMLRLGAEY
     RLYPCPLFSV RYRKPLFGET GHTIMNLLAD FRNYQYTLPV VQGLVVDMEV RKTSIKIPSN
     RYNEMMKAMN KSNEHVLAGG ACFNEKADSH LVCVQNDDGN YQTQAISIHN QPRKVTGASF
     FVFSGALKPS SGYLAKSSIV EDGVMVQITA ENMDSLRQAL REMKDFTITC GKADAEDPQE
     HIHIQWVDDD KNVNKGVISP IDGKSMESIT SVKIFHGSEY KANGKVIRWT EVFFLENDDQ
     HNCLSDPADH SRLTEHVAKA FCLALCPHLK LLKEDGMTKL GLRVTLDADQ VGYQAGSNGQ
     PLPSQYMNDL DSALVPVIHG GACQLSEGPV VMELIFYILE NIA
//
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