ZFY26_AILME
ID ZFY26_AILME Reviewed; 2543 AA.
AC D2H5P6;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Zinc finger FYVE domain-containing protein 26;
GN Name=ZFYVE26; ORFNames=PANDA_005234;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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; GL192509; EFB24961.1; -; Genomic_DNA.
DR RefSeq; XP_011220351.1; XM_011222049.2.
DR AlphaFoldDB; D2H5P6; -.
DR STRING; 9646.ENSAMEP00000015112; -.
DR PRIDE; D2H5P6; -.
DR Ensembl; ENSAMET00000015733; ENSAMEP00000015112; ENSAMEG00000014294.
DR GeneID; 100468320; -.
DR KEGG; aml:100468320; -.
DR CTD; 23503; -.
DR eggNOG; KOG1811; Eukaryota.
DR HOGENOM; CLU_228199_0_0_1; -.
DR InParanoid; D2H5P6; -.
DR OrthoDB; 1237900at2759; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
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; 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; 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; 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..2543
FT /note="Zinc finger FYVE domain-containing protein 26"
FT /id="PRO_0000408350"
FT ZN_FING 1816..1876
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 523..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1272..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1780..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 870..897
FT /evidence="ECO:0000255"
FT COMPBIAS 786..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1791..1811
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1825
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1839
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1842
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1847
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1850
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A8G9"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 1744
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU37"
FT MOD_RES 1765
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68DK2"
FT MOD_RES 1784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU37"
FT MOD_RES 1786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DU37"
SQ SEQUENCE 2543 AA; 283930 MW; A589BB2417A0D2E3 CRC64;
MHHPFGKEET ASQKQLFGFF CECLRRGEWE LAQACVPQLH EAQGDIPKKV EDILQALVVC
PDQLRCGQDI DPQRLAWVWF LVLEKWFSQE KKLLPSVFRR KLEFLLLSED LRRDIPEDIL
KELYEALAQD TGGPVLDGNQ KRESWTPRLS SEAVSVFWDL LRQAPQLAQA LLELLRTKDD
SAGLSGWSLQ KALVDRVRRA LGAVQGPTTG PAGIVDAIYG ALRSLRCPAE PLGGELRLLC
EELLEACRAE GSPLQEEQVL SCLLHKAGRS LVSLYGHIYA EKATEKPAKA VHLGKVSPDH
LDPEQAMLAL FCNPDPSQAW KSAYFYCLSN SKHFLEQILV TALALLKEED FPSLGCLLDR
EFRPLSRLLV LLGWMHCQSL ASAKRLLQTL HRAQDQGCDK LLRDACDGLW AHLEVLEWCV
QQSSNPIPKR DLLCHLHGGD SHSVLYSLHH LTNLPALREE DVLKLLQKVP AKDPQQEQDS
AEAPVPEHLS RCQNLTLYQS FCAMKYAIYA LCVNSHQHSQ CQECRDSPSE DPALAAEPAN
DSLSSPGASD LFSTYLARCQ QYLCNVPDSL CLELLENIFS LLLITSADLH PEPHLPEDYA
EDEDIEGKGL LGLRSPSESP QHIAQPERKS EQGCQEVPRS LACTVPNCLK TEPKESSPGL
HGHSFLDLKH FTSGISGFLA DEFAIGAFFR LLQEQLDKLS SHSPPEKPKL PEGQSCSGSR
DGLQSRLHRF SKVLSEAQWR YKVVTSNQGS EEQPSRRYWP IATGHPSLRR GRRTRRSRPD
GRDRSSNPSL ESTSSELSTS TSEGSLNAVS GRNELDGRLQ PQSQNSLIPM MFSPPESLLA
SCILRGNFAE AHQVVFMFNL KSSPSSGELM FMERYQEVIQ ELSRVEHKIE NQNSDGGSST
IRRTGSGRST LQAIGSAAAA GMVFYSISDV TDKLLSTSGE PIPTLQEDFW ISNTLVEPTA
PLREVLEDLS PPAMAAFDLA CSQCQLWKTC KQLLETAERR LNVSLESRGR RLDHILLSAD
GIRGFPVVLQ QISKILNYPL TSAGQSKSES VEEKGAGPPR CSIAELLQMC WPSLTEDCVA
SHATLSQQLD QVLQVLREAL QRPEPRSTPL SSLVEQAAQK APEAEAHPVH IQTQLLQKNL
GKQTPAGSRQ TDYMGTFFSY CNTMAAVLLR SLSSEPDHME VKVGNPFVLL QQSSSQLVSH
LLLERQVPPD RLAALLAREG LSLSVPKVIV NCCCEPLALC SSRQSQQTSS LLTHLDVLVQ
LHTSHCLEDL PLSTLSSPKP TGNSTLERKP HSSPRDSSLP AFTSSALAFL KSRSKLLATV
ACLGASQGPK LTKPSLSWKE LRGRREVPLS AEQVAQECER LLEQFPMLKA SLLAAWEPLR
RSTEQGQSLA VSLCGRASLS TVLLGLHSPS ALDVLTEAFE EALVARDWSR ALQLTEVYGR
DVDDLSNIKD AVLSCATACD KEGWRFLFPV KDASLRSRLT LQFVDRWPLE WCLEILAYCI
SDTAVQGGLK CELQRKLAEL RVYQKILGLQ ATPVWCDWQS LRNCCIEDPS AVMNMILEAK
EYGLCEEWGC LYPIPREHLI SLHQKHLLHL LERGDHEKAL QLLRKIPDPT MCLEVTEQSL
DQHPSLAASH FLANYLTTHF YGELTAVRHH EIQALYMGSK VLLTLPEPHR ASYSHLSSNP
LLMLEQLLMN MKVDWATVAV QTLHQLLAGQ EIGFTMDDID SLLSIYAGKA LDFPYSLREK
RSDSLTHLQE VSQPSDLVTL SRSPSGEFSV AAAVAAPGVS TIHSPSPRER SFPESQPPPE
FVPPATPPGR PQWVPDESAS ICMVCCRERF TMFNRRHHCR RCGRLVCSAC STKKMVVEGC
RESPTRVCDQ CYSYYNKDVP EENAGQPEAP DSSKSESPPY SAVVRVPKAA EVEWILDLNE
EENELVRSEF YYEQSPSASL CIAILNLHRD SIACGHQLIE HCCRLSQGLT NPEVDAGLLT
DIMKQLLFSA KMMFVKAGRS QDLALCDSYI SKVDVLNILV AASYRHVPPL DQILQPAAVT
RLRNQLLEAE YYQLGVEIST KTGLDPTGAW HAWGMACLKA GNLTAAREKF GRCLKPPFDL
NQLSHGSRLV QDVVEYLEST VRPLLSLQDD DYFATLKELE ATLRTQSLSL EVIPEGKIMN
NTYYQECLFY LHNYSTNLAI ISFYMRHSCM REALLHLLNK ESPPEVFIEG IFQPSYKSGK
LHTLENLLES IDPTLETWGK YLIAACQHLQ KKNYYHILYE LQQFMKDQVR AAMTCIRFFS
HKAKTYTELG EKLSWLLKAK DHLKIYLQDT SRSTRRKKTT FFQKKMTAAD VSRHMNTLQL
QMEVTRFLHR CESAGTSQIT TLPLPTLFGN NHMKMDVACK VMLGGKNVED GFGIAFRVLQ
DFQLDAAATY CRAARQLVER EKYSEIQQLL KCVSESGMAA TSDGDTILLN CLEAFKRIPP
QELEGLIQAI HSDDNKVQAY LTCCKLRSAY LIAVKQEHSR ATVLVQQVQQ AAKSSGDAVV
QDICAQWLLT SHTRGSHGSG SRK
