ZFY26_BOVIN
ID ZFY26_BOVIN Reviewed; 2515 AA.
AC E1BLZ4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Zinc finger FYVE domain-containing protein 26;
GN Name=ZFYVE26;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
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; AAFC03015524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03064315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BLZ4; -.
DR SMR; E1BLZ4; -.
DR STRING; 9913.ENSBTAP00000040846; -.
DR PaxDb; E1BLZ4; -.
DR PRIDE; E1BLZ4; -.
DR eggNOG; KOG1811; Eukaryota.
DR HOGENOM; CLU_228199_0_0_1; -.
DR InParanoid; E1BLZ4; -.
DR OrthoDB; 1237900at2759; -.
DR TreeFam; TF324517; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
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 3: Inferred from homology;
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..2515
FT /note="Zinc finger FYVE domain-containing protein 26"
FT /id="PRO_0000408351"
FT ZN_FING 1788..1848
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 520..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 842..869
FT /evidence="ECO:0000255"
FT COMPBIAS 586..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1794
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1797
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1822
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1840
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1843
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 1718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU37"
FT MOD_RES 1740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 1756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU37"
FT MOD_RES 1758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU37"
SQ SEQUENCE 2515 AA; 280355 MW; 55D6346300C2C465 CRC64;
MHHPFGKEEA ASQKQLLGFF CECLRRGEWE LAKACVPQLH EAQGDIPKKV EDILWALVLC
PNQLRCGQDI SPQRLAWVWL LVLEKWLALE KKLLPTGFRR KLEFLLLSED LPSDISEDIL
KELYAVLAQD RVDPVLDGNL RQESWPPRLS SEAVSMLWDL LREAPQVAQA LLELLLGEVD
GAGLRGWPLQ KALVDLIRKA LRTLQGPTAA PPGTVDAIYG ALRTLRCPAE PLGAELRLLC
EELLEACRSE GSPLREERLL GCLLHKAGRD LVSLYSHTYA EKATPSGKVP PDPLDPERAM
LALFSNPDPA HAWKVAYFYC LSNSKHFLEQ ILVTALTLLK EEDFPSLGCL LSREFRPLSR
LLVLLGWTHC QSLASAKSLL QTLHRTQDQG CDKLLRDACD GLWAHLEVLE WCVQHSSNPI
PKRDLLCHLH GGDSHSVLYS LHHLTNLPAL REEDVLKLLQ KVPAKDPQQE HDSADTLVPA
HLSQSQSLTL YRSFCAMKYA IYALCVSSHQ HSQCRQCKDG PSDDLASVAE PMNDPPSSPG
ASDLFSTYLA RCQQYLCSIP DSLCLELLEN VFSLLLITSA DLHPEPHLPE DYAEDAQPER
KSEQGALGTA RGLAYTVPSC PKPEPKDSSP EPHGHSFLDL KHFTSSVSGF LADEFAIGAF
LRLLQEQLDE LSSRGPPEKP KLLEDQSGSG SRDGLQSRLH QFSKVLSEAQ WRYKVVTSIQ
GSEEQPSRRY RPITTRHPSL RRGRRTRKSR ADDQDKGSRS SLENTSSELS TSTSEGSLSA
ASGKNELEGR LQPQPHSSLI PMMFSPPESL LASCILRGNF AEAHQVVFTF NLKSSHGSGE
LMFMERYQEV IQELAQVEHK IENQNSDGGS STIRRTGSGR STLQAIGSAA AAGMVFYSIS
DVTDKLLSTS GDPIPTLQED FWISSCPMEL TAPLKEVLED LSPPAMAAFD LACSQCQLWK
TGKQLLETAE RRLNSSLESQ GRRLDHVFVN ADGIRGFPGV LQQISKILNY PLVSAGQIKS
ESGEDKGGGP PRCSIAELLQ MCWPSLTEDC VASHTTLSQQ LEQILQSLRE ALELPEPRST
PLSSLVEQVA QKAPEAEAHP VYIQAQLLQK NLGKQTAAGG KQTDYMGTFF RYCSTLAAVL
LRSLSSEPDH VEVKVGNPFV LLQQSSSQLV SHLLLERQVP PDRLAALLAQ EGLSLSVPQV
IVNCCCEPLT LCSSRQSKQT SALLTRLGTL AQLHTSRCLD DLPLSTLSCL KSTENPTLER
KPPSSPRDSS PPALTSSALA FLKSRSKLLA TVACLGASRG SKVTKTSLSW KELRGRREVP
LTAEQVAREC ERLLEQFPVL EASLLAAWEP LRGSSEQGQS LASSLCGQAS LSTVLLGPHS
PTALDVLTEA FEEALVARDW RRALQLTDVY GQDVDDLSSI QDAVLSCAAA CDKEGWQFLF
AVKDACLRSQ LTLQFVDRWP LEWCLEILAY CLSDTAVQDG LECELRRKLA ELQVYQKILG
LQSTPVWCNW QALRNCCAED PSTVMNLILE AKEYELCEEW GCLYPIPREH LINLHQKHLL
HLLERGDHEK ALQQQLLQRI PDPTMCLEVT EQSLDQHPSL ATSHFLANYL TTHFYGELTA
DRHREIQALY MGSKVLLTLP EQHRASYAHL SSSPLLMLEQ LLMNMKVDWA AVAVQTLRQL
LAGQEIGFTT DEVDALLSRY AGKALDFPYP LREKRSDSVI HLQEIVSQVS DLETLSRSPS
AEFSSATAPG VSTVHSPSVR ERNFPPSQLP LEFVPPATPP ARHQWVPDES ESVCMVCRRE
RFTMFNRRHH CRRCGRLVCS SCSTKKMVVE GCRENPTRVC DQCYSYFNQD VPEENPGQAE
APDSSKSESP PYSAVVRVPK AAEVEWILDL NEEENELVRS EFYYEQAPSA SLCIAILNLH
EDSVSCGHQL IEHCCRLSQG LTNPEVDAGL LTDIMKQLLF SAKMMFVKAG QSQDLALCDS
YISKVDVLNI LVAAAYRHVP SLDQILQPAA VTRLRNQLLE AEYYQLGVEV STKTGLDPTG
AWHAWGMACL KAGNLTAARE KFSRCLKPPF DLNQLSHGSR LVQEVVEYLE STARPLLSVQ
DDDFLATLKE LEATLRTQSL SLEVIPEGKI LNNTYYQECL FYLHSYSTHL AIISFYVRHS
CLREALLHLL HTESPPEVFI EGIFQPSYKS GKLHDLENLL ESIDSSLESW GKYLIAACQH
LQKKNYYHIL YELQQFMKDH VRAAMTCIRF FTHKAKTYTE LGEKLSWLLK AKDHLKIYLQ
ETSRRSGRKK TTFFRKKMTA SDVSRHMNTL QLQMEVTRFL HRCESAGTSQ VTTSPLPTLF
GNNHMKMDVA CKVMLGGKNV EDGFGIAFRV LQDFQLDAAA TYCKAARQLV EREKFGEIRQ
LLKCVSESGM AAQSDRDTVL LNCVEAFRRI PPQELEGLIQ AIHSDDNKVQ AYLKCCKLRS
AYLIAVKQEH SRAAVLVEQV QQAAKSSGDA VVQDICSQWL LTSRSRGAHG SASRK
