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Database: UniProt
Entry: A0A2K5NDV7_CERAT
LinkDB: A0A2K5NDV7_CERAT
Original site: A0A2K5NDV7_CERAT 
ID   A0A2K5NDV7_CERAT        Unreviewed;      1380 AA.
AC   A0A2K5NDV7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Zinc finger FYVE domain-containing protein {ECO:0000256|PIRNR:PIRNR037289};
GN   Name=ZFYVE9 {ECO:0000313|Ensembl:ENSCATP00000035505.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000035505.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000035505.1}
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   Ensembl; ENSCATT00000059788.1; ENSCATP00000035505.1; ENSCATG00000040598.1.
DR   GeneTree; ENSGT00940000154290; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000040598; Expressed in frontal cortex and 12 other cell types or tissues.
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:UP000233060};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          699..758
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          200..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1380 AA;  151448 MW;  46A799AE3CC22069 CRC64;
     MENYFQAEAY NLDKVLDEFE QNEDETVSST LLDTKWNKIL DPSSHRLSFN PTLASVNESA
     VSNESQPQLK VFSLAHSAPL TTEEEDHCAN GQDCNLNPEI ATMWIDENAV AEDQLIKRNY
     SRDDQCSAVE VGEKKCGNLT CLPDEKNVLV VAVMHNCDKR TLQNDLQDCN NYNSQSLMDA
     FSCSLDNENR QTDQFSFSIN ESTEKDMNSE KQLDPLNRPK IEGNSVNHLC ATSSDSLASG
     CSPSQLKDDG NIGRDPSISA ITNLTVDSVI SSHGTDGGPA IRKQENYIPD EDLTGKISSP
     RTDLGSPNSF SHMSEGILTK KEPAEESTTE ESLRSGLPLL LKPDVPNGSG RNNDCERFSD
     CIVPSEVRAG ENEGYEHEEI LGTTEFLNMT EHFSESQDMT NWKLTKLNEM NDSQVNEEKE
     KFLQISQPED TNGDSGGQCV GLADAGLDLK GTCISESEEC DFSTVIDTPA ANSLYNGCDS
     YGMQGPGVSF VPKTLPSKED SVTEEKEIEE SKSECYSNIY EQRGNEATEG SGLLLNSTGD
     LMKKNYLRNF CSQVPSVLGQ SSPKVVASLP SISVPFGGAR PKQPSNLKLQ IPKPLSDHLQ
     NDLPANSGNN TKNKNDILGK AKLGENSATN VCGASLGNIS NVDTNGEHLE SYEAEISSRP
     CLALAPDSPD NDLRAGQFGI SARKPFTTLG EVAPVWVPDS QAPNCMKCEA RFTFTKRRHH
     CRACGKVFCA SCCSLKCKLL YMDRKEARVC VICHSVLMNA QAWENMMSAS SQSPNPNNPA
     EYCSTIPPLQ QAQASGALSS PPPTVMVPVG VLKHPGAEVA QPREQRRVWF ADGILPNGEV
     ADAAKLTMNG TSSAGTLAVS HDPVKPVTTS PLPAETDICL FSGSITQVGS PVGSAMNLIP
     EDGLPPILIS TGVKGDYAVE EKPSQISVMQ QLEDGGPDPL VFVLNANLLS MVKIVNYVNR
     KCWCFTTKGM HAVGQSEIVI LLQCLPDEKC LPKDIFNHFV QLYRDALAGN VVSNLGHSFF
     SQSFLGSKEH GGFLYVTSTY QSLQDLVLPT PPYLFGILIQ KWETPWAKVF PIRLMLRLGA
     EYRLYPCPLF SVRFRKPLFG ETGHTIMNLL ADFRNYQYTL PVVQGLVVDM EVRKTSIKIP
     SNRYNEMMKA MNKSNEHVLA GGACFNEKAD SHLVCVQNDD GNYQTQAISI HNQPRKVTGA
     SFFVFSGALK SSSGYLAKSS IVEDGVMVQI TAENMDSLRQ ALREMKDFTI TCGKADAEDP
     QEHIHIQWVD DDKNVSKGVI SPIDGKSMET ITNVKIFHGS EYKANGKVIR WTEVFFLEND
     DQHNCLSDPA DHSRLTEHVA KAFCLALCPH LKLLKEDGMT KLGLRVTLDS DQVRCVFRSF
//
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