ID A0A3Q0DBA7_MESAU Unreviewed; 1479 AA.
AC A0A3Q0DBA7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=FYVE and coiled-coil domain-containing protein 1 {ECO:0000313|RefSeq:XP_021089894.1};
GN Name=Fyco1 {ECO:0000313|RefSeq:XP_021089894.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021089894.1};
RN [1] {ECO:0000313|RefSeq:XP_021089894.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=28071753;
RA McCann K.E., Sinkiewicz D.M., Norvelle A., Huhman K.L.;
RT "De novo assembly, annotation, and characterization of the whole brain
RT transcriptome of male and female Syrian hamsters.";
RL Sci. Rep. 7:40472-40472(2017).
RN [2] {ECO:0000313|RefSeq:XP_021089894.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_021089894.1; XM_021234235.1.
DR STRING; 10036.ENSMAUP00000021211; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15726; FYVE_FYCO1; 1.
DR CDD; cd17698; RUN_FYCO1; 1.
DR Gene3D; 1.20.58.900; -; 1.
DR Gene3D; 2.60.120.680; GOLD domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR047337; FYVE_FYCO1.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR047336; RUN_FYCO1.
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; PTHR46753; FYVE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR46753:SF2; FYVE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF140741; RUN domain-like; 1.
DR SUPFAM; SSF101576; Supernatant protein factor (SPF), C-terminal domain; 1.
DR PROSITE; PS50866; GOLD; 1.
DR PROSITE; PS50826; RUN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 74..207
FT /note="RUN"
FT /evidence="ECO:0000259|PROSITE:PS50826"
FT DOMAIN 1177..1235
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1338..1467
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 1237..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 270..304
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 347..374
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 423..579
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 627..887
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 923..1151
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1239..1271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1479 AA; 167139 MW; B4B88DDAF3EEB18A CRC64;
MSWCQNVPPW SLITADWQPH STEVKAYRGP THPRKGDTMA SSNTETQLQR IIRDLQDAVT
ELSNEFKEGG EPITDDSTSL HKFSYKLEYL LQFDQKEKTS LLGSKKDYWD YFCACLAKVK
GANDGIRFVR SISELRTSLG KGRAFIRYSL VHQRLADTLQ QCFMNTKVTS DWYYARSPFL
KPKLSSDIVG QLYELTEVQF DLASRGYDLD AAWPTFARRT LGTGSSAYMW KPPSRSSSMS
SLVSNYLQTQ EMASGFDINN PLNNEGLEGF DEMRLELDQL EVREKQLQEH VQQLDRENQA
LRVMISRQGE QLEVEKERGY PMVEGTIGLM GLVAELQKQG EVIQATVKKL QTCLQALELN
VDKKESNYSA LQLETLAQEL EAVRDSLGRK NQLLASLSDC LARAEKDRKF HQEPVPADMA
LEFQELKGKL EALEGENTKA QELNMQQSIK LEQLAKELQL KEEARAGLEH SVKAVAPLEE
ELSAKKQESA QLRRQLQESL AHLSSVEEEL AEARQQAKQH REERQLREQE AKSLTWQLQL
LETQLAQVSQ LVSDLEEQKK QLVQDRDRLS QKVGTLEQLA EVRGVPLSSV PPQTEEMLEE
EVQYRHKEHV SNTTVPGGDQ EKLGKVNQEL QKELQNMAVR NQLLEGKLQA LQTDYKALQQ
REAAIQGSLA SLEAEQASIR HLGDQMEASL LAVKRVKETM KAQVAEKEAA LQSKEGECQR
LQEEADQCRL RTEAQDQELR ALENQCQQQI QLIEALSAEK GHQGLSLPQV NTAQLALSQA
QLEVHRGEAQ RLQNEVVDLQ AKLQVALGDR DKLQSQLGVT EAVLREHKTL VQQLKEQNEA
LNRAHVQELL QCSEREGILQ EESIYKTQEQ EQELQALHAE LSQVRCSSEG AHLEHAELQD
QLHRANTDTA ELGIQVCALT AEKDRMEGAL ATLAHELQDT KEAALQERKG LELQVRGLQQ
EKESLQEKLK AAEEAASSFS GLQAQLVQAE QLTQSLQEAA HQERDALKFQ LSAEIMGHQN
RLKAANEECG SLRAQLEEQS RQLEMTKEAV RELKVTKAAM EEKLNSTSSH LAECQATLQH
KDEESATLRI SLERTQKELE KATSKIQEYY NKLCQEVTNR ERNDQKMLAD LDDLNRTKRY
LEERLIELLR DKDALWQKSD ALEFQQKLSA EEKGLGDMEA NHCHDCKREF SWIVRRHHCR
ICGRIFCYYC CNNYAVTKPS GKKERCCRAC FQKFGEGPGS PDSSGSGTSQ GEPSPMVSPA
EAGSQAQGVN SVCRPPDDAV FDIITDEELC QIQESGSSLP ETPTETDSMD PNMAEQDTTS
NSLTPEDTED MPMGQDAEIC LLKSGELMIK LPLTVDEITS FGEGNRELFV RSSTYSLIPI
TVAEPGLTIS WVFSSDPKSI SFSVVFQETE DTPLDQCKVL IPTTRCNSHK ESIRGQLKVR
TPGIYLLIFD NTFSRFISKK VFYHLTVDRP VIYDGSDFP
//
