ID A0A3B3RG79_9TELE Unreviewed; 2355 AA.
AC A0A3B3RG79;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Zinc finger FYVE domain-containing protein 26 {ECO:0000256|ARBA:ARBA00014373};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000016890.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000016890.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Phosphatidylinositol 3-phosphate-binding protein required for
CC the abcission step in cytokinesis: recruited to the midbody during
CC cytokinesis and acts as a regulator of abcission. May also be required
CC for efficient homologous recombination DNA double-strand break repair.
CC {ECO:0000256|ARBA:ARBA00025209}.
CC -!- SUBUNIT: Interacts with AP5Z1, AP5B1, AP5S1 and SPG11. Interacts with
CC TTC19 and KIF13A. {ECO:0000256|ARBA:ARBA00025962}.
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DR STRING; 1676925.ENSPKIP00000016890; -.
DR Ensembl; ENSPKIT00000041393.1; ENSPKIP00000016890.1; ENSPKIG00000002954.1.
DR GeneTree; ENSGT00920000149143; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR GO; GO:0048599; P:oocyte development; IEA:Ensembl.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR028730; ZFYVE26.
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; PTHR46591; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 26; 1.
DR PANTHER; PTHR46591:SF1; ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 26; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 1667..1727
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 621..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2110..2132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2155..2177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..660
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2355 AA; 261023 MW; 99ACC33D8647F12F CRC64;
MNLLGKKEDS SMEQLFSFFT LCLQCGDWEL AQACVPQLNN TTCTSTQCLQ DILKSLVTCP
YELQPVLSVC LSQELHQAFR SVQIEKKGTM VILSAEAECC LGTLLDRSRP RLAQALVHFL
QGHRADDDAC DRKHLLQEAF IQFLLAKVQQ SGQAEVGWEE KLYSALAVMP WGPEPVEGQL
HDLCRALWAA STGPLSEERV LSSLLRPRCH AALSFYYLTE AGKLMLGLCC HAERASAWKA
IYFECLSSNK HFLDQVLITA LDLIRREEFS RLKDLTAAEF HPLSRLLLLL GWTHLQSLGS
AQKLLETLHH SQALANDSVL KDFVDGLSSQ LGVLEWCAKN TILHVLNSPL INNDDASLLG
DTDTAHPVDT PNLSARRNVV LFQGFCAMKY ALYAICVNAH KYSGCRDCLV AKEPFFLSLA
PSGFSVLFQY YLSECQLYLE AVPALFRLEL LENIFSLLFL SSADFVLSRE RDIEHGLPHE
QYLPSRCGLE KSDNPEFRKE SKGGGVVVDW TLQQPQQPGR HTLQNLVCNY VDLGHFIQDC
KGFLVDTVAM EGFLRLLRES LEGVCVVGQR DGLEEGRALA GEEEMAESLG CSVTPETFGT
RLQRLSKRIA EAHWRLQVIT SNHGSSSNGQ IPTTKLVSRV PSLKHNGGMK RRKKSRRHRT
ERHSTAEQHN GEVSTSTSDG SVGVAGAPAE QEPCPCGGPH SWLIPAMLSS PESLLISCIR
RGNFLEAHQV SLMFGLDGSA CSGELVFMEH HRDVLVELGC VEQKIENQVA DGSASGRSRL
GSSGRSTLQA IGSAAAAGMA FYSISDMADM LLSTPGRPVP SLEEDYWLNH KVPDPSGVLH
ALLEEFSPAS MATFDLACCH CLLWKTSRQL LETAERRLNT TLEGRGVRTD STVPHSHGIK
GFPAVLQQIS KIINHSVSGK GSPRAGMGIL FLNASDFFFT WVLHQYHISV SDPVFLCPDG
RVGGGLLAAL VEQASFKQSE LDSHPVRSQM KQLLRTLDQL CPSEPDSAPF RPDYVRSFLD
YVNTLAVVLV RSLSSEGKVE VKLGNPLLVL LQLPSQLVSH LLFDRQVSPI RVSSLLEQEG
LGLNIQQVIV QRCCETLPVW ETCCESMGET GRKTGGLLSL NSVKVFLQKY SQEHPLTVCP
STNSSQSSPA SSSSSSSLLL TPSSLSFLKS HSPILAVLAC LSACRGGAGR TGSAWPGLPA
YFRSGRKEGV LDIEQVAREA EALLKDLPIL HAYLQTMAQP VLGPVGSPEG SGAVSGLSAS
LCGLPLAGLL LSGLHRASAC SAAAGAFQQA LTDRDVERAL NLLELYGQDS HQEQKLRDSL
LACSALREGN RTMEHLFRVE DAELRARVAL QGLEQWPLAS CLELLRFCLS DGNTECSLKE
ELELKKQELQ IYQRFRLNHA GSALLPHVIP LIYFACPSCQ EFQLCGQWVQ LYPVSMQLRL
QLQTEHLLHL LERGQMEEAF QLLESLTDSA LCLEVCEHAL DRRPGLAACH FLADYLTLHF
QDGMSPARRH LIHALHLGSK VLLTLPPDAQ EDYFPLLSNP LLMLEQLLMN LKVDWAAVAV
RTLRGLLLGQ ECIISPGDID ALLSSYARKA LEFPYAPRER TRSDSVISLQ DVLTQTFCRT
SLSLWFHVIA GSTPVHTPCA GGGRRTKPTA YFTPPEKPPS RKDWIPDHQQ SVCMVCLRER
FTMFNRRHHC RRCGRLVCQA CSGHRMPLEG FAEDTSRVCN QCYGFFHPLL SSSFTLQGPS
SSLCIAILSL HSDHVACGHQ LIDHCHSLSR GLTNPEVDAR LLTDIMRQLL FSAKLMFVKA
GQNQDLALCD SYISKVDVLK ILVVANYKYV PSLDDISESA AITRLRNQLL EAEYYQLAVE
VSTKSALDPG GVWHAWGIAS LKAGSLTIAR EKFARCLKAP VDRNQLNHGP RLLREIIQHL
ESTVWSSHTQ VQDILASLRE LEETLADPGS QDNSNGQGQQ NCYYEECLYY LHHYGTHLAI
VSFYMRHDDM KGALLHLRSK ECPEEVFLEG VLQPSLEQGR LGALQGLLEG LDPSLENWSR
YLIASCQFLQ RRGHFHTLYQ LQQFMMDHVR AAMTCIRFFA HGAKSYLQLG EQQRWLVRAK
EHLRTYLQEQ QGRCSSRRKS SSTFRKKMSS SDVSRHMNTI ELQLEVTRFL HRCESSAGPG
HAPQAQPPAS NAPPPTLFEG SSMKVDVACK VMLGGKNIEE GFGIAYRVIQ DFQLESPAVY
VRTGQWLVRQ RQYGAVRQLL KCVGESGAAT KNDCDRIVLS CVSAADKGPA KELESLILES
KSVENKINGY LLCSKLRAAY LLAVKLEPGR AGPLVAEVMQ AAEKTGDSIM QDICRQWLAE
HQDRPPRQQV RSNAR
//