ZFY26_RAT
ID ZFY26_RAT Reviewed; 2542 AA.
AC D4A8G9; D3ZB97; D3ZBA4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Zinc finger FYVE domain-containing protein 26;
GN Name=Zfyve26;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612 AND SER-616, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AP5Z1, AP5B1, AP5S1 and SPG11. Interacts with
CC TTC19 and KIF13A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Midbody {ECO:0000250}. Note=Localizes
CC to the centrosome during all stages of the cell cycle. Recruited to the
CC midbody during cytokinesis by KIF13A (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The FYVE-type zinc finger mediates binding to
CC phosphatidylinositol 3-phosphate and recruitment to the midbody during
CC cytokinesis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZFYVE26 family. {ECO:0000305}.
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DR EMBL; CH473947; EDM03727.1; -; Genomic_DNA.
DR RefSeq; NP_001101508.1; NM_001108038.1.
DR AlphaFoldDB; D4A8G9; -.
DR STRING; 10116.ENSRNOP00000016380; -.
DR iPTMnet; D4A8G9; -.
DR PhosphoSitePlus; D4A8G9; -.
DR PaxDb; D4A8G9; -.
DR PeptideAtlas; D4A8G9; -.
DR PRIDE; D4A8G9; -.
DR GeneID; 314265; -.
DR KEGG; rno:314265; -.
DR UCSC; RGD:1307820; rat.
DR CTD; 23503; -.
DR RGD; 1307820; Zfyve26.
DR eggNOG; KOG1811; Eukaryota.
DR InParanoid; D4A8G9; -.
DR OrthoDB; 1237900at2759; -.
DR PhylomeDB; D4A8G9; -.
DR TreeFam; TF324517; -.
DR PRO; PR:D4A8G9; -.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 6.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:1905037; P:autophagosome organization; ISO:RGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:RGD.
DR GO; GO:0007040; P:lysosome organization; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 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; PTHR46591; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW DNA damage; DNA repair; Lipid-binding; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..2542
FT /note="Zinc finger FYVE domain-containing protein 26"
FT /id="PRO_0000408352"
FT ZN_FING 1815..1875
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 591..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1746..1807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 866..891
FT /evidence="ECO:0000255"
FT COILED 1495..1522
FT /evidence="ECO:0000255"
FT COMPBIAS 756..773
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1821
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1824
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1838
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1841
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1846
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1849
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1867
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1870
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 1739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU37"
FT MOD_RES 1761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 1783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU37"
FT MOD_RES 1785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU37"
SQ SEQUENCE 2542 AA; 284215 MW; 3128C41C447CBD11 CRC64;
MSYPFGKEET TTEKQLFEFF CECLRRGDWE LAQACVPQLQ RGQGEIPQKV EDILQALVQC
PILLRCGPDI NPQRLAWLWL LVLEKWLPPE KKLLSTVFRR KLEFLFLSED LQGGIPETIL
KELFETLAQG PAGCTSDRSQ RWESGAPQLS PEAVSMLWNL LKQAPGPAQA LLELLLEERH
SASLCHSSLQ KSLLDLIRKA LQTLRDPASQ PAGVTDAVCG ALQALCCTAE LPEGEWHVLC
EELLETCRTE GSPLKEERLL GCLLHKAGRS LLSLYGHTYA EKVAERPPKA SLSGKDHPDP
ERAMLALFST PDPAHAWKMA FFYCLSNNKH FLEQILVTAL TLLKEEDFPS LGYLLDREFR
PLSHLLVLLG WTHCQSLESA KRLLQTLYRN QDQGHDELLR DACEGLWAHL EVLEWCVQQS
SSLIPKRELL CHLHGGDSHS VLYSLHHLTN LPALREEEVL KLLQKVPTKD LQGEHDTHDA
SVPEHLSQCQ SLTLYQGFCA MKYAVYALCV NSHQHSQCPD CRDSASSEEL ALVEPGRDSL
PSPGASHLFP TYLARCRQYL QRIPDSLCLE ILENIFSLLL ITSADLHPEP HLPEDYAEDD
DIEGKGPWGL WSPSESPQHI AATERRSERA SMGPRDLAPT GPGCPKGEPK DNSPGPHTHS
FLDLKHFTSS LSGFLADEFA IGAFLSLIQE QLNELSSHRT PEETELLEDQ SCWAARDGLQ
GRLHRFSKVL SEAQWRYKVV TSNQSSEEQP SRRYRPTAKR HSSLRRGRRT RRTRADGRER
GSNPSLEGTS SELSTSTSEG SLSAVSGQVE ADNRFQPQPQ SSIIPMMFSP PESLLASCIL
RGNFAEAHQV VLMFNLKSSP SAGELMFVER YQEVIQELAR VEHKIENQNS DGGNNTVRRT
GSGRSTLQAI GSAAAAGMVF YSISDVTDKL LSPSEDPIPT LQEDFWINAA LTETNTPLRG
VLEDLSPPAM AAFDLACCQC QLWKTCKQLL ETAERRLSSS LEGRGRRLDQ VVLNPDGMRG
FPFVLQQISK ILSYPLTVTG LTKSETLEER GGGAPRCSIS ELLQMCWPSL TEDCIASHTS
LSQQLDQALQ SLREALTLSE PKSTPLTCLV EQAAQKAPEA EAHPVHIQSQ LLQKTLGKQT
LAGPRQTDYV GAFFSYCSSL AKVLLRSLSS DPDNVEVKVG NPFVLLQQSS SQLVSHLLLE
RQVPPDRLAA LLAQEHLNLS VPQVIVSCCC EPLTLCLSRQ SQQASSLTAH LGMLAQGHAS
HLLDGLPLSV LGSPRPSENP SAERKSDSSP KDSLPAFTAS ALAFLKSRSK ILAMVACLRA
SRGTKVSRPS LSWKELRGRR EAPLTAEKVA QECEHLLEQF PVFEAALLAN WEPLQQASES
RPSLAASLCG QARLSTVLLG LHSTLAQDVV TEAFEEALVA RDWPRALQLI DVYGQDSDDL
SSVRDSVLTC ATVCDKEGWQ YLFPVKDASL RSQLALRFVD KWPLESCLEI LAYCVSDMAV
PEELKSELQR KLTELRVYQK ILGLQDPPVW CDWQTLRSCC AEDPSTVMDM MLGSQEYELC
EEWGCLYPIP REHLVSLHHK HLLYLLERRE YEKALQLLQR IPDPTMCLEV TERSLDQHPS
LATSHFLANY LTSHFYGELT TDRHHEIQAL YMGSKVLLTL PEQHRASYAH LSSSPLLMLE
QLLMNMKVDW ATTAVQTLQQ LLAGQDIGFT LDEVDSLLSR YAGKALDLPY PLREKRSDSM
IHLQEPVHQA SDPETLSRSS SAEFSAAAAA PAPAAPGSAL VCSPSPKERA FPQTQPPLEF
VPPETPPARD QWVPDETESM CMVCCREHFT MFNRRHHCRR CGRLVCGSCS TKKMVVEGCR
ENPTRVCDQC YSYYNKDAPE ESPCQSEVPD SAKNESPSYS AVVRIPKATE VEWILSLNEE
ENELVRSEFY YEQAPSASLC IAILNLHRDS IACGHQLIEH CCRLSRGLTN PEVDAGLLID
IMKQLLFSAK MMFVKAGQSQ DLALCDSYIS KVDVLHILVA AAYRHMPSLD QILQPASVTR
LRNQLLEAEY YQLGVEVSTK TGLDSTGAWH AWGMACLKAG NLTAAREKFS RCLKPPLDLN
QLSHGSRLVQ DVVEYLESTV RPLVSLQDDD YFATLRELEA TLRTQSLFLE AIPDGKIMNN
TYYQECLFYL HNYSTNLAII SFYMRHNCLR EALLHLLNKE SPAEVFIEGI FQPSYKSGKL
HTLENLLESI DPTLESWGAY LIAACQHLQK KNYYHILYEL QQFMKDQVRA AMTCIRFFSH
KAKSYTELGE KLSWLLKAKD HLKIYLQENS RSSGRKKTTF FRKKMAAADV SRHMNTLQLQ
MEVTRFLHRC ESARTSQITT LPLPTLFGNN HMKMEVACQV MLGGKNVEDG FGIAFRVLQD
FQLDAAVTYC RAARQLVEKE KYGEIRQLLK CVSESGMAAK SDGDTILLNC LEAFKRIPPQ
ELEGLIQAIH SDDNKVRAYL TCCKLRSAYL IAVKQEHTQA AALVQQVQQA AKSSGDSVVQ
DICAQWLLTS HSRGAHGSGS RK
