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Database: UniProt
Entry: A0A2K5K1S7_COLAP
LinkDB: A0A2K5K1S7_COLAP
Original site: A0A2K5K1S7_COLAP 
ID   A0A2K5K1S7_COLAP        Unreviewed;      1498 AA.
AC   A0A2K5K1S7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=FYVE and coiled-coil domain autophagy adaptor 1 {ECO:0008006|Google:ProtNLM};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000035051.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000035051.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; XP_011808062.1; XM_011952672.1.
DR   STRING; 336983.ENSCANP00000035051; -.
DR   Ensembl; ENSCANT00000058287.1; ENSCANP00000035051.1; ENSCANG00000041209.1.
DR   GeneID; 105519333; -.
DR   KEGG; cang:105519333; -.
DR   CTD; 79443; -.
DR   OrthoDB; 5394846at2759; -.
DR   Proteomes; UP000233080; 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:UP000233080};
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          584..615
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          400..441
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        586..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1233..1250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1498 AA;  168840 MW;  3A89049B465895B8 CRC64;
     MASTNAESQL QRIIRDLQDA VTELSKEFQE AGEPITDDST SLHKFSYKLE YLLQFDQKEK
     ATLLGNKKDY WDYFCACLAK VKGANDGIRF VKSISELRTS LGKGRAFIRY SLVHQRLADT
     LQQCFMNTKV TSDWYYSRSP FLQPKLSSDI VGQLYELTEV QFDLASRGYD LDAAWPTFAR
     RTLATGSSAY LWKPPSRSSS MSSLVSSYLQ TQEMVSNFDL NSPLNNEALE GFDEMRLELD
     QLEVREKQLQ ERIQQLDREN QELRAAVSLQ GEQLQTERER GRTAAEDNVR LTCLVAELQK
     QWEVTQATQN TVKELQTCLQ ALELGAAEKE EDYHTALRQL ESMLQPLAQE LKATWDPLGK
     KNQHLASIPD WLVMAQQKAD TAPDTKGQQE PIPSDAAQEI QELGEKLRTL ERERTKVEEV
     NRQQSAQLEQ LVKELQLKED AWASLEHLVK EMAPLQEELS GKGQEADQLW RRLQELLVHS
     SSREQELAEL RREKKQQQEE KELLEQEVRS LTRQLQFLET QLAQVSQHVS DLEEQKKQLI
     QDKDHLSQKV GALERLAGQP SPELPVAGGK NEALVPVNSS LQEACGKPEE EQRGPQEAQL
     DDTKVQEGSQ EEELRQANRE LEKELQNVVG RNQLLEGKLQ ALQADYQALQ QREAAIQGSL
     ASLEAEQASI RHLGDQMEAS LLAVRKAKEA MKAKVAEKEA TLQSKEDECQ QLREEVEQCR
     QLAEARHREL RALESQCQQQ TQLIEVLTAE KGQQGVGPPP DDEARELAAQ LALSQAQLEV
     HQGEAQRLQA QVVDLQAKMR AALDDQDKMQ SQLSMAEAVL REHKTLVQQL KEQNEALNRA
     HVQELLQCSE REGALQEERT SEAQQREEEL RALQEELSQA KCSSEEAHLE HAELQEQLHR
     ANTDTAELGI QVCTLTMEKE QVEKALASAV QELQDAKEAA SREREGLERQ VAGLQQEKES
     LQEKLKVAQA AADSLPGLQA QLTQAEQRAQ SLQEAAHQEL DTLKFQLSAE IMDYQSRLKN
     AGEESRSLRG QLEEQGRQLQ AAEEAVGKLK ATQADMGEKL SCTSNHLAEC QAAMLRKDKE
     GAALREDLER TQKELEKAAT KIQEYYNKLC EEVTNRERSD QKMLADLDDL NRTKKYLEER
     LIELLRDKDA LWQKSDALEF QQKLSAEDRW LGDTEANHCL DCKREFSWMM RRHHCRICGR
     IFCYYCCNNY VLSKHSGKKE RCCRACFQKL SEGPGSPDST GSGTSQGEPS PAPSPASPGP
     QATGGQGANT DYRPPDDAVF DIITDEELCQ IQESGSSLPE TPTETDSLDP NVAEQASAGA
     SKGLGNLLCE SSAYRDTTST SLTPEDTEDM PVGQDAEICL LKSGELMIKV PLTVDEIASF
     GEGSRELFVR SSTYSLIPIT VAEAGLTISW VFSSDPKSIS FSVVFQEAED TPLDQCKVLI
     PTTRCNSHKE NIQGQLKVRT PGIYMLIFDN TFSRFVSKKV FYHLTVDRPV IYDGSDFL
//
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