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Database: UniProt
Entry: G3RH65_GORGO
LinkDB: G3RH65_GORGO
Original site: G3RH65_GORGO 
ID   G3RH65_GORGO            Unreviewed;      2530 AA.
AC   G3RH65;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Zinc finger FYVE domain-containing protein 26 {ECO:0000256|ARBA:ARBA00014373};
GN   Name=ZFYVE26 {ECO:0000313|Ensembl:ENSGGOP00000014981.3};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000014981.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000014981.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000014981.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000014981.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; CABD030092949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030092950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9593.ENSGGOP00000014981; -.
DR   Ensembl; ENSGGOT00000015409.3; ENSGGOP00000014981.3; ENSGGOG00000015342.3.
DR   eggNOG; KOG1811; Eukaryota.
DR   GeneTree; ENSGT00920000149143; -.
DR   HOGENOM; CLU_228199_0_0_1; -.
DR   InParanoid; G3RH65; -.
DR   OMA; DWATMAV; -.
DR   TreeFam; TF324517; -.
DR   Proteomes; UP000001519; Chromosome 14.
DR   Bgee; ENSGGOG00000015342; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR   GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:1905037; P:autophagosome organization; IEA:Ensembl.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR   GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR   GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR   CDD; cd15724; FYVE_ZFY26; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          1803..1863
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   REGION          594..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          699..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1258..1287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1746..1799
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1866..1885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..723
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..770
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        771..797
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1259..1276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2530 AA;  283286 MW;  51B89815B3DC97DB CRC64;
     MNHPFGKEEA ASQKQLFGFF CECLRRGEWE LAQACVPQLQ EGQGDIPKRV EDILQALVVC
     PNLLRCGQDI NPQRVAWVWL LVLEKWLARE KKLLPFVFRR KLEFLLLSED LQGDIPENIL
     EELYETLTQG AVGHVPDGNP RRESWTPRLS SEAVSVLWDL LRQSPQPAQA LLELLLGEDD
     GTGLCHWPLQ NALVDLIRKA LRALQGPDSV PPGVVDAIYG ALRTLRCPAE PLGVELRLLC
     EELLEACRTE GSPLREERLL SCLLHKASRG LLSLYGHTYA EKVTEKPPRA TASGKVSPDH
     LDPERAMLAL FSNPNPAEAW KVAYFYCLSN NKHFLEQILV TALTLLKEED FPNLGCLLDR
     EFRPLSCLLV LLGWTHCQSL ESAKRLLQTL HRTQGPGCDE LLRDACDGLW AHLEVLEWCI
     QQSSNPIPKR DLLYHLHGGD SHSVLYTLHH LTNLPALREE DVLKLLQKVP AKDPQQEPDA
     VDAPVPEHLS QCQNLTLYQG FCAMKYAIYA LCVNSHQHSQ CQDCKDSLSE DLASATEPAN
     DSLSSPGAAN LFSTYLARCQ QYLCSIPDSL CLELLENIFS LLLITSADLH PEPHLPEDYA
     EDDDIEGKSP SGLRSPSESP QHIAHPERKS ERGSLGVPKT LAYTMPSHVK AEPKDSYPGP
     HRHSFLDLKH FTSGISGFLA DEFTIGAFLR LLQEQLDEIS SRSPPEKPKQ ESQSCSGSRD
     GLQSRLHRLS KVVSEAQWRH KVVTSNHRSG ERRVELVGPE GGEGERSQEY GREGSNPSLE
     STSSELSTST SEGSLSAMSG RNELHSRLHP HPQSSLIPMM FSPPESLLAS CILRGNFAEA
     HQVLFTFNLK SSPSSGELMF MERYQEVIQE LAQVEHKIEN QNSDAGSSTI RRTGSGRSTL
     QAIGSAAAAG MVFYSISDVT DKLLNTSGDP IPMLQEDFWI STALVEPTAP LREVLEDLSP
     PAMAAFDLAC SQCQLWKTCK QLLETAERRL NSSLERRGRR IDHVLLNADG IRGFPVVLQQ
     ISKSLNYLLM SASQTKSESV EEKGGGPPRC SITELLQMCW PSLTEDCVAS HTTLSQQLDQ
     VLQSLREALE LPEPRTPPLS SLVEQAAQKA PEAEAHPVQI QTQLLQKNLG KQTPSGSRQM
     DYLGTFFSYC STLAAVLLQS LSSEPDHVEV KVGNPFVLLQ QSSSQLVSHL LFERQVPPER
     LAALLAQENL SLSVPQVIVS CCCEPLALCS SRQSQQTSSL LTRLGTLAQL HASHCLDDLP
     LSTPSSPRTT ENPILERKPY SSPRDSSLPA LTSSALTFLK SRSKLLATVA CLGASPRLKV
     SKPSLSWKEL RGRREVPLAA EQVARECERL LEQFPLFEAF LLATWEPLRG SLQQGQSLAV
     NLCGWASLST VLLGLHSPIA LDVLSEAFEE SLVARDWSRA LQLTEVYGRD VDDLSSIKDA
     VLSCAVACDK EGWQYLFPVK DASLRSRLAL QFVDRWPLES CLEILAYCIS DTAVQEGLKC
     ELQRKLAELQ VYQKILGLQS PPVWCDWQTL RSCCVEDPST VMNMILEAQE YELCEEWGCL
     YPIPREHLIS LHQKHLLHLL ERRDHDKALQ LLRRIPDPTM CLEVTEQSLD QHTSLATSHF
     LANYLTTHFY GQLTAVRHRE IQALYVGSKI LLTLPEQHRA SYSHLSSNPL FMLEQLLMNM
     KVDWATVAVQ TLQQLLVGQE IGFTMDEVDS LLSRYAEKAL DLPYPQREKR SDSMIHLQEI
     VHQAADPETL PRSPSAEFSP AAPPGISSIH SPSLRERSFP PTQPTQEFVP PATPPARHQW
     VPDETESICM VCCREHFTMF NRRHHCRRCG RLVCSSCSTK KMVVEGCREN PARVCDQCYS
     YCNKDVPEEP SEKPEALDSS KSESPPYSFV VRVPKADEVE WILDLKEEEN ELVRSEFYYE
     QAPSASLCIA ILNLHRDSIA CGHQLIEHCC RLSKGLTNPE VDAGLLTDIM KQLLFSAKMM
     FVKAGQSQDL ALCDSYISKV DVLNILVAAA YRHVPSLDQI LQPAAVTRLR NQLLEAEYYQ
     LGVEVSTKTG LDTTGAWHAW GMACLKAGNL TAAREKFSRC LKLPFDLNQL NHGSRLVQDV
     VEYLESTVRP LVSLQDDDYF ATLRELEATL RTQSLSLAVI PEGKIMNNTY YQECLFYLHN
     YSTNLAIISF YVRHSCLREA LLHLLNKESP PEVFIEGIFQ PSYKSGKLHT LENLLESIDP
     TLESWGKYLI AACQHLQKKN YYHILYELQQ FMKDQVRAAM TCIRFFSHKA KSYTELGEKL
     SWLLKAKDHL KIYLQETSRS SGRKKTTFFR KKMTAADVSR HMNTLQLQME VTRFLHRCES
     AGTSQITTLP LPTLFGNNHM KMDVACKVML GGKNVEDGFG IAFRVLQDFQ LDAAMTYCRA
     ARQLVEKEKY SEIQQLLKCV SESGMAAKSD GDTILLNCLE AFKRIPPQEL EGLIQAIHND
     DNKVRAYLIC CKLRSAYLIA VKQEHSRATA LVQQVQQAAK SSGDAVVQDI CAQWLLTSHP
     QGAHGSGSRK
//
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