ID A0A2K5EQS4_AOTNA Unreviewed; 1425 AA.
AC A0A2K5EQS4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Zinc finger FYVE domain-containing protein {ECO:0000256|PIRNR:PIRNR037289};
GN Name=ZFYVE9 {ECO:0000313|Ensembl:ENSANAP00000035559.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000035559.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000035559.1}
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_012290054.1; XM_012434631.1.
DR STRING; 37293.ENSANAP00000035559; -.
DR Ensembl; ENSANAT00000053628.1; ENSANAP00000035559.1; ENSANAG00000035282.1.
DR GeneID; 105705051; -.
DR CTD; 9372; -.
DR GeneTree; ENSGT00940000154290; -.
DR OMA; IPPNCGG; -.
DR OrthoDB; 3061552at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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:UP000233020};
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..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..352
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 1425 AA; 156163 MW; 92C751D15E882476 CRC64;
MENYFQAEAY NLDKVLDEFE QNEDETVSST LLDTKWNKIL DPTSHRLSFN AALASVNESA
VSNESQPQLK VFSLAHSAPL TTEEEDHCAN GQDCNLNPEI ATMWIDENAV TEDQLIKRNY
SRDDQCSAVE VGEKKCENLA CLPDEKNVLV VAVMHNCDKR TLQNDLQDCN NYNSQSLMDA
FSCSLDNENR QTDQFSFSIN ESTEKDMNSE KQMDPLNRPK IEGSSVNHLC ATSSDSLASV
CSPSQLKDDG SIGGDPSMST ITSLTVDSVI SSQGTDGGPV IKKQENCIPD EDLTGKISSP
RTDLGSPNSF SDMNEGILMN KEPAEESTTE ESLRSGLPLL LKPDVPNGSG RDNDCERFSD
FLVPSEVRAV ENEGYEHEEI LGTIEFLNIT EHFSESQDLT NWKLTKLNEM NDSQINEEKE
KFLQISQPED TNGDSGGQCV GLADAGLDLK GTCISESEEC DFSTVIDTPA ANSLSNGCDS
YGMQSPSVSF VQKTLPSKED SVTEEKEIEE SKSECYSNIY EQRGNEATEG SGLLLNSTGD
LMKKNYLRNF CNQVPSVLGQ SSPKLVASLP SISVPFGGAR PKQPSNLKLQ IPKPLSDHLQ
NDLPANSGNN TKNKNDILGK AKLGENSATN VCSASLGNIS NVDTNGEHLE NYEAEISNRP
CLALAPDSPD NDLRAGQFGI SARKPFTTLG EVAPVWVPDS QAPNCMKCEA RFTFTKRRHH
CRACGKVFCA SCCSLKCKLL YMDRKEARVC VICHSVLMNA QAWENMMSAS SQSPNPNNPA
EYCSTIPPLQ QAQASGALSS PPPTVMVPVG VLKHPGAEVA QPREQRRVWF ADGILPNGEV
ADAAKLTMNG TSSAGTLAVS HDPVKPVTTS PLPAETDISL FSGNITQVGS PVGSAMNLIP
EDGLPPILIS TGVKGDYAVE EKPSQISVMQ QLEDGGPDPL VFVLNANLLS MVKIVNYVNR
KCWCFTTKGM HAVGQSEIVI LLQCLPDEKC LPKDIFNHFV QLYRDALAGN VVGNLGHSFF
SQSFLGSKEH GGFLYVTSTY QSLQDLVLPT PPYLFGILIQ KWETPWAKVF PIRLMLRLGA
EYRLYPCPLF SVRFRKPLFG ETGHTIMNLL ADFRNYQYTL PVVQGLVIDM EVRKTSIKIP
SNRYNEMMKA MNKSNEHVLA GGACFNEKAD SHLVCVQNDD GNYQTQAISI HNQPRKVTGA
SFFVFSGALK SSSGYLAKSS IVEDGVMVQI TAENMDSLRQ ALREMKDFTI TCGKADAEDP
QEHIHIQWVD DDKNVSKGVV SPIDGKSMET ITNVKIFHGS EYKANGKVIR WTEVFFLEND
DQHNCLSDPA DHSRLTEHVA KAFCLALCPH LKLLKEDGMT KLGLRVTLDS DQVGYQAGSN
GQPLPSQYMN DLDSALVPVI HGGACQLSEG PVVMELIFYI LENIA
//
