ID A0A2K5EB56_AOTNA Unreviewed; 1498 AA.
AC A0A2K5EB56;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=FYVE and coiled-coil domain autophagy adaptor 1 {ECO:0000313|Ensembl:ENSANAP00000030390.1};
GN Name=FYCO1 {ECO:0000313|Ensembl:ENSANAP00000030390.1};
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:ENSANAP00000030390.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000030390.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 37293.ENSANAP00000030390; -.
DR Ensembl; ENSANAT00000048428.1; ENSANAP00000030390.1; ENSANAG00000032948.1.
DR GeneTree; ENSGT00940000154044; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005776; C:autophagosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; IEA:Ensembl.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; IEA:Ensembl.
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:UP000233020};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 36..169
FT /note="RUN"
FT /evidence="ECO:0000259|PROSITE:PS50826"
FT DOMAIN 1173..1231
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1357..1486
FT /note="GOLD"
FT /evidence="ECO:0000259|PROSITE:PS50866"
FT REGION 593..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 225..273
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 393..556
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1081..1147
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 934..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1498 AA; 169164 MW; A7262813A5FEDDF2 CRC64;
MASTNAESQL QRIIRDLQDA VTELSKEFQE AGEPVTDDST SLHKFSYKLE YLLQFDQKEK
ATLLGNKKDY WDYFCACLSK VKGANDGIRF VKSISELRTS LGKGRAFIRY SLVHQRLADT
LQQCFMNTKV TSDWYYARSP FLQPKLSSDI VGQLYELTEV QFDLASRGYD LDAAWPTFAR
RTLATGSSAY LWKPPSRSSS MSSLMSSYLQ TQEMASNFDL NSPLNNEALE GFDEMRLELD
QLEVREKQLQ ERMQQLDREN QELRAAVSLQ GQQLQTERER GRTAAEDNVR LTCLVAELQK
QREVTQATQN TVKELQMCLQ ALELGAAEKE EDYHTALQQL ESLLQPLAQE LETTRDSLGK
RNQHLASIPD RLAMAQQKAD AAPDTKGQQE PIPSDAAREI QELQEKLRAL ERKRTKVEEV
NRQQSAQLEQ LAKELQLKED TQANLERLVK EVAPLQEELS GKGQEADQLC QRLQELLAHS
RSREEELAEL RREEKQRQEE KELLEQEVTS LTRQLQFLET QLAQVNQHVS DLEEEKKQLI
QDKDHLSQKV GALERLAGQP GPELPVADEK NETLVPVNSP LQVACGKLEE EQRSLQGAQL
DDTKVQEGSQ EEELRQANRE LEKELQNVVG RNQLLEGKLQ ALQADYQALQ QRETAIQGSL
ASLEAEQASI RHLGEQMEAS LLAVRKAKKA MKAQVAEKEA TLQSKEGECQ QLREEVEQYR
QLAEARHREL RALESQCHQQ TQLIEVLTAE KDQQGVSPLP DSEAHELAAQ LAVSQAQLEV
HQGEAQRLQA QVVDLQAKMR AALDDRDKVQ SQLSMAEAVL SEHKTLVQQL KEQNEALNRA
HVQELLQCSE REGMLQEERT GEAQQREEEL RALQEELSQA KCSSEEAQLE HAELQEQLHR
ANTDTAELGI QVCALTMEKE RVEEALANAV QELRDSKEAA SREREGLERQ VAGLQQEKES
LQEKLKAAKT EASSLPGLQA QLAQAEQRAQ SLQEAAHQEL DTLKFQLSAE IMDYQNRLKN
AGEECRNLRG QLEEQGRQLQ AAEEAVGKLK ATQADMGEKL NCTSNHLAEC QAAMLRKDQE
GAALREDLER TQKELEKASI KIQEYYNKLC QEVTDRERND QKMLADLDDL NRTKKYLEER
LIELLRDKDA LWQKSDALEF QQKLSAEDRW LGDTEANHCL DCKREFSWMV RRHHCRICGR
IFCYYCCNNY VLTKHSGKKE RCCRACFQKL SEGPGSPDST GSGTSQGEPS PALSPASAGP
QATGHQGANT DYRPPDDAVF DIITDEELCQ LQEFGSSLPE TPTETDSLDP NVAEHTSARA
SKGLGNLLCE SSACLDTTST SLTPEDTEGM PVGQDAEICL LKSGELMIKV PLTVEEIASF
GEGSRELFVR SSTYSLIPIT VAEAGLTISW VFSSDPKSIS FSVVFQEAED TPLDECKVLI
PTTRCNSHKE NIQGQLKVRT PGIYMLIFDN TFSRFVSKKV FYHLTVDRPV IYDGSDFL
//
