ID M3Y761_MUSPF Unreviewed; 2539 AA.
AC M3Y761;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Zinc finger FYVE domain-containing protein 26 {ECO:0000256|ARBA:ARBA00014373};
GN Name=ZFYVE26 {ECO:0000313|Ensembl:ENSMPUP00000007165.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000007165.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000007165.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-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; AEYP01004123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01004126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004739055.1; XM_004738998.2.
DR STRING; 9669.ENSMPUP00000007165; -.
DR Ensembl; ENSMPUT00000007284.1; ENSMPUP00000007165.1; ENSMPUG00000007223.1.
DR GeneID; 101673216; -.
DR KEGG; mpuf:101673216; -.
DR CTD; 23503; -.
DR eggNOG; KOG1811; Eukaryota.
DR GeneTree; ENSGT00920000149143; -.
DR HOGENOM; CLU_228199_0_0_1; -.
DR InParanoid; M3Y761; -.
DR OMA; DWATMAV; -.
DR OrthoDB; 2945465at2759; -.
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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 1809..1869
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 519..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1801
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2539 AA; 283566 MW; 09E54D61A194DFE6 CRC64;
MHHPFGKEET ASQKQLFGFF CECLRRGEWE LAQACVPQLH EAQGDIPKKV EHILQALVVC
PDQLRCGQDM NPQRLAWVWF LVLEKWFSQE KKLLPSVFRR KLEFLLLSEN LQRDIPENIL
KEFYEALAQD TGGPVLDGNQ RRESWSPRLS SEAISVLWDL LRQAPQAAQA LLELLLHEDD
GTGTLQKALV DLIRRALGAV QGPTAGPGGI VDAIYGALRS LHCPAEPLGV ELRLLCEELL
EACRAGGSPL REEHVLNCLL HKAGRSLVSL YGHIYAEKAT EKPVKAVPSG KVSPDHLDPE
QAMLALFSNP DPAQAWKSAY FYCLSNSKHF LEQILVTALA LLKEEDFPSL GHLLDREFRP
LSRLLVLLGW THCQSLASAK RLLQTLHRAQ DQGCDKLLRD ACDGLWAHLE VLEWCVQQSS
NPIPKRDLLS HLYGGDSHSV LYSLHHLTNL PALREEDVLK LLQKVPAKDP QQEHDSAGAP
VPEHLSRCPN LTLYQSFCAM KYAIYALCVN SHQHSQCREC RDSPSEDPAM AAEPENDSLS
SPGASDLFST YLARCQQYLC SIPDALCLEL LENIFSLLLI TSAELHPEPH LPEDYAEDDD
IEGKGLLDLR SPSESPQHAA QPERKSERGC QGVPRSLANT IPSCPKTEPK DSSPGPHGHS
FLDLKHFTSG ISGFLADEFA IGAFLRLLQE QLDKLNSHSP PEKPKLLEGQ SCSGSRDGLQ
SRLQRFSKVL SEAQWRYKVV TSNQSSEEQP SRRYRPMATG HPSLRRGRRT RKSRPDGRDR
SSNPSLESTS SELSTSTSEG SLNAVSGRNE LDGRLQPQSQ SSFIPMMFSP PESLLASCIL
RGNFAEAHQV VFMFNLKSSP SSGELMFMER YQEVIQELSR VEHKIENQNS DGGSSTIRRT
GSGRSTLQAI GNAAAAGMVF YSISDVTDKL LSTSGEPIPT LQEDFWISNS LVEPTAPLRE
VLEDLSPPAM AAFDLACSQC QLWKTCKQLL ETAERRLNIS LESRGRRLDH VVLNADGIRG
FPVVLQQISK ILNYPLTSTG QTKPESIEEK GAGPPRCSVA ELLQLCWPSL TEDCVASRAT
LSQQLDQVLQ SLREALQLPE PRSTPLSSLV EQAAQKAPEA EAHPVYIQTQ LLQKNLDKHT
PAGSRQTNYM GTFFSYCSTM AAVLLRSLSS EPDHVEVKVG NPFVLLQQSS SQLVSHLLLE
RQVPPDRLAA LLAREGLSLS VPKVIVNCCC EPLALCSSRQ NQQTSSLLTH LGVLVRLHTS
QCLEDLPLST LGSPKPTGNS TVERKPRSSP RESSLPALTS SALAFLKSRS KLLALVACLG
ASQGPKLTKP SLSWKEFRGR REVPLSAEQV AQECERLLEQ FPVLRASLLA AWEPLRRSTE
QGQSLAANLC GRASLSTVLL GLHSPTALQV LTEAFEEALV ARDWTRALQL TEAYGRDVDD
LSNIKDAVLS CAAACDKEGW QFLFPVKDAS LRSRLTLQLV DRWPLEWCLE ILAYCISDTT
VQDGLKCELQ RKLAELRVYQ KILGLQSTPV WCDWQSLRNC CIEDPSTVMN MILEAKEYGL
CEEWGDLYPI PREHLVSLHQ KHLLHLLERG DHEKALQLLR RIPDPTMCLE VTEQSLDQHP
SLAASHFLAN YLTTHFYGEL TAVRHREIQA LYMGSKVLLT LPEPHRASYS HLSSNPLLML
EQLLMNMKVD WATVAVQTLH QLLAGQEIGF TMDDVDSLLS RYAGKALDFP YSLREKRSDS
VTHLPEVGQT SDLETLSRSP SAEFSAAAAP GVSTIHSPSP RERSFPESQP PPEFVPPAAP
PGRHQWVPDE SESICMVCCR ERFTMFNRRH HCRRCGRLVC SACSTKKMAV EGCRESPTRV
CDQCYSYYNK DVPEENPGQP EAPDSSKSES PPYSAVVRVP KAAEVEWILD LNEEENELVR
SEFYYEQSPS ASLCIAILNL HRDSIACGHQ LIEHCCRLSQ GLTNPEVDAG LLTDIMKQLL
FSAKMMFVKA GRSQDLALCD SYISKVDVLN ILVAASYRHV PPLDQILQPA AVTRLRNQLL
EAEYYQLGVE ISTKTGLDPT GAWHAWGMAC LKAGNLTAAR EKFSRCLKPP FDLNQLSHGS
RLVQDVVEYL ESTVRPLLSL QDDDYFATLK ELEVTLRTQS LSLEVIPEGK IMNNTYYQEC
LFYLHNYSTN LAIISFYMRH NCLREALLHL LNKESPPEVF IEGIFQPSYK SGKLHTLENL
LESIDPTLES WGKYLIAACQ HLQKKNYYHI LYELQQFMKD QVRAAMTCIR FFSHKAKTYT
ELGEKLSWLL KAKDHLKIYL QDTSRSTRKK KTTFFQKKMT AADVSRHMNT LQLQMEVTRF
LHRCESAGTS QITTLPLPTL FGNNHMKMDV ACKVMLGGKN VEDGFGIAFR VLQDFQLDAA
ATYCRAARQL VEREKYGEIQ QLLKCVSESG MAARSDGDTI LLNCLEAFKR IPPQELESLI
QAIHSDDNKV QAYLTCCKLR SAYLIAVKQE HSRATALVQQ VQQAAKSSGD AVVQDICAQW
LLTSHTRAAP QAHGSGSRK
//
