ID A0A2K6QHS6_RHIRO Unreviewed; 1498 AA.
AC A0A2K6QHS6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=FYVE and coiled-coil domain autophagy adaptor 1 {ECO:0000313|Ensembl:ENSRROP00000028331.1};
GN Name=FYCO1 {ECO:0000313|Ensembl:ENSRROP00000028331.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000028331.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000028331.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 61622.ENSRROP00000028331; -.
DR Ensembl; ENSRROT00000052680.1; ENSRROP00000028331.1; ENSRROG00000037953.1.
DR GeneTree; ENSGT00940000154044; -.
DR Proteomes; UP000233200; 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:UP000233200};
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 588..610
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 REGION 1294..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 225..273
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 400..448
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 473..556
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1081..1147
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1233..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1498 AA; 169031 MW; EA6CDA9BA9C36192 CRC64;
MASTNAESQL QRIIRDLQDA VTELSKEFQE AGEPITDDST SLHKFSYKLE YLLQFDQKEK
ATLLGNKKDY WDYFCACLAK VKGANDGIRF VKSISELRTS LGKGRAFIRY SLVHQRLADT
LQQCFMNTKV TSDWYYARSP FLQPKLSSDI VGQLYELTEV QFDLASRGYD LDAAWPTFAR
RTLATGSSAY LWKPPSRSSS MSSLVSSYLQ TQEMVSNFDL NSPLNNEALE GFDEMRLELD
QLEVREKQLQ ERMQQLDREN QELRAAVSLQ GEQLQTERER GRTAAEDNVR LTCLVAELQK
QWEVTQATQN TVKELQTCLQ ALELGAAEKE EDYHTALRQL ESMLQPLAQE LKATRDSLGK
KNQHLASIPD WLAMAQQKAD TAPDTKGQQE PIPSDAAQEI QELGEKLRAL EREKTKVEEV
NRQQSAQLEQ LVKELQLKED AWASLERLVK EMAPLQEELS GKGQEADQLW RRLQELLVHS
SSWEQELAEL RREKKQQQEE KELLEQEVRS LTRQLQFLET QLAQVSQHVS DLEEQKKQLI
QDKDHLSQKV GALERLAGQP GPELPVAGGK NEALVPVNSS LQEACGKPEE EQKGLQEAQL
DDTKVQEGSQ EEELRQANRE LEKELKNVVE RNQLLEGKLQ ALQADYQALQ QREAAIQGSL
ASLEAEQASI RHLGDQMEAS LLAVRKAKEA MKAKVAEKEA TLQSKEDECQ QLREEVEQCR
QLAEARHREL RALESQCQQQ TQLIEVLTAE KGQQGVGPPP DDEARELAAQ LALSQAQLEV
HQGEAQRLQA QVVDLQAKMR AALDDQDKMQ SQLSMAEAVL REHKTLVQQL KEQNEALNRA
HVQELLQCSE REGALQEERT SEAQQREEEL QALQEELSQA RCSSEEAQLE HAELQEQLHR
ANTDTAELGI QVCTLTMEKE QVEEALACAV QELQDAKEAA SREREGLERQ VAGLQQEKES
LQEKLKVAKA AADSLPGLQA QLTQAEQRAQ SLQEAARQEL DTLKFQLSAE IMEYQSRLKN
AGEESRSLRG QLEEQGRQLQ AAEEAVGKLK ATQADMGEKL SCTSNHLAEC QAAMLRKDKE
GAALREDLER TQKELEKATT KIQEYYNKLC QEVTNRERSD QKMLADLDDL NRTKKYLEER
LIELLRDKDA LWQKSDALEF QQKLSAEDRW LGDTEANHCL DCKREFSWMM RRHHCRICGR
IFCYYCCNNY VLSKHSGKKE RCCRACFQKL SEGPGSPDST GSGTSQGEPS PALSPASPGP
QATGGQGANT DYRPPDDAVF DIITDEELCQ IQESGSSLPE TPTETDSLDP NVAEQASTGT
SKGLGNLLCE SFAYRDTTST SLTPEDTEDM PVGQDAEICL LKSGELMIKV PLTVDEIASF
GEGSRELFVR SSTYSLIPIT VAEAGLTISW VFSSDPKSIS FSVVFQEAED TPLDQCKVLI
PTTRCNSHKE NIQGQLKVRM PGIYMLIFDN TFSRFVSKKV FYHLTVDRPV IYDGSDFL
//
