ID S7NCF5_MYOBR Unreviewed; 2723 AA.
AC S7NCF5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Zinc finger FYVE domain-containing protein 26 {ECO:0000256|ARBA:ARBA00014373};
GN ORFNames=D623_10024701 {ECO:0000313|EMBL:EPQ14969.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ14969.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC {ECO:0000256|ARBA:ARBA00005647}.
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DR EMBL; KE164080; EPQ14969.1; -; Genomic_DNA.
DR eggNOG; KOG1811; Eukaryota.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR CDD; cd15724; FYVE_ZFY26; 1.
DR Gene3D; 2.30.170.20; Ribosomal protein L24e; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR038630; L24e/L24_sf.
DR InterPro; IPR000988; Ribosomal_eL24-rel.
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 Pfam; PF01246; Ribosomal_L24e; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 1926..1986
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 625..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1989..2010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1873..1889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2723 AA; 303831 MW; 4F465C4C44493C6E CRC64;
MHYPFGKEET ASQRELFGFF CECLQRGEWE LAQACVPQLH AAQGDIPKQV EDILRALVAC
PHQLRCGPDI NPQRLAWVWL LVLEKWFAQE KPRMMFIRNN CKVFRFCKSK CDKNFKKKLN
PYKKLLPAVF RRKLEFLLLS EDLQGNIPED ILKELYEALS QDTADPVLDE NQRPESRTLR
LSSEAVSVLL DLLSQASQPA QALLELLLRE DDGPGPGGWP LQKALVDLIR KALRALQDAA
PGSPGGVEAI YGALRTLRCP AEPLGAELRL LCEELLEACR TEGSPLQEER LLSCLLHKAG
RGLLSLYGHA YAEKAAMKPL KASSLGEVSP DHLDPERAML ALFSNPDSAE AWKLAYFYCL
SNSKHFLEQI LVTALTLLKE EDFPSLGCLL DREFRPLRRL LVLLGWTHCQ SLASARRLLQ
TLHRTQDQGG DKLLRDACDG LWAHLEVLEW CVQQSSSPIP KRDLLCHLHG GDSHSVLYSL
HHLTNLPALR EEEVLKLLQK VPAKEPQQEH NSAGAPGPEH LSQCQNLTLY RSFCAMKYAI
YALCVNSHQH TQCQECKDSL SEDLAVAAEP MNDSVPPSGA SNLFSTYLAR CQQYLCGVPD
SLRLELLENI FSLLLMTSAD LHPEPHLPED YAEEDDIDGK DPLGLGSPPE SPQHIAQPER
KSERGSLGVP RSLADTLPSC LKTEPKDSSP EPHGHSFLDL EHLTSGVSGF LADEFAMGAF
LRLLQDQLEE LSSHSPPEDP MLPEGQNCPE SRHGPQSRLH RFSKVLSEAQ WRYKVVTSNQ
SSEEQPFRRY RPVATWHPSL RRGRRTRRSR ADGRDRGSNP SLESTSSELS TSTSEGSLNI
MSGRNELQPQ TQSSFIPMMF SPPESLLASC ILRGNFAEAH QVVFMFDLKS SPSSGELMFV
ERYQEVIQEL ARVEHKIENQ NSDGGSSTIR RTGSGRSTLQ AIGSAAAAGM VFYSISDVTD
KLLSPSGDPI PTLQEDFWIS STLLEPTDPL REVLEELSPP AMAAFDLACS QCQLWKTCKQ
LLETAERRLN SSLESRGMVF YSISDVTDKL LSPSGDPIPT LQEDFWISST LLEPTDPLRE
VLEELSPPAM AAFDLACSQC QLWKTCKQLL ETAERRLNSS LESRGRQLDH VLPSADGIRG
FPVVLQQISK ILNYLLTSAG QTKSESIEEK GGGLPRCSIA ELLQTCWPSL TEDCAASHAT
LSQQLDQILQ SLREALELPE PRSSPLSSLV EQAAQKAVET EAHPVHIQTE LLQKTLGRQA
PVGSGQTDYM GTFSSYCSTL AAVLVQSLRS EPDHVEVRVG NPFVLLQQSS SQLVSHLLLE
RQVPPDRLAA LLAREGLSLS VPQVIVNCCC EPLALCPSLQ SQQMSSLLTH LGILAQLHTS
HCLEDLPLSA QSSPKPTENP TSEKKPSSSK DSSPSALTSS ALAFLKSRSK LLATVACLGA
SRGSKVTKPS LSWKELRGRR EVPLTAEQVA RECVRLLEQF PMLEASLLAA WEPLRGSSKQ
EQSLAASLCG QASLSTVLLG LHSPVALDVL TEAFKEALVA RDWPRALQLT EVYGQDMDDL
SSIRDAVLSC AVASDEEGWQ YLFPVKDASL RSQLTLKFVD RWPLESCLEI LAYCISDTTV
PAELRCELQR KLAELQMYQK ILGLQATPVW CDWQTLRNCC VDDPSTVMNV ILEAKEYGLC
EEWGCLYPIP REHLISLHQR HLLYLLEGGD HEKALQLLRR IPDPSMCLEV TEQSLDQHPS
LATSHFLANY LTTHFYGKLT AVRHCEIQAL YMGSKVLLTL PEQHRASYSH LSSKPLLMLE
QLLMNMKVDW ATMAVQTLHP LLARQEIGFT MDDVDSLLSR YAGKALDFPY SLLHGIHLQE
TVGQASDLET LTRSPSAEFS PTTAPGQGVA IVRSPSPKER SVPQSQPPLE FVPPATPPGR
HQWVPDESES LCMVCCREHF TMFNRRHHCR RCGRLVCSSC STKKMVVEGY RENPTRVCDQ
CYGYYNKDEP EENPGQPEAP DSAKNESPPY SAVVRVPKAP EVEWILDLNE EENELVRNEF
YYEQAPSASL CIAILNLHRD SVACGHQLIE HCCRLSQGLA NPEVDAGLLT DIMKQLLFSA
KVMFVKAGRS QDLALCDSYI SKVDVLNILV AAAYRHVPSL DQILQPAAVT RLRNQLLEAE
YYQLGVEVST KTGLDPTGAW HAWGMACLKA GNLTAAREKF SRCLKPPFDL NQLSHGSRLV
QDVVEYLEST VRPLLSLVST KTGLDPTGAW HAWGMACLKA GNLTAAREKF SRCLKPPFDL
NQLSHGSRLV QDVVEYLEST VRPLLSLQDD DYLATLKELE ATLRTQSLSL EVIPEGKIMN
NTYYQECLFY LHNYSTNLAI VSFYVRHSCL REALLHLLNK ESPPEVFIEG IFQPSYKSGK
LHVLENLLES IDPTLECWGE YLLAACQHLQ KKNYYHILYE LQQFMKDQVR AAMTCIRFFS
HKAKTYTELG EKLSWLLKAK DHLKIYLQET SRSSKRKKTN FFRKKMTAAD VSRHMNTLQL
QMEVTRFLHR CESAGTSQIT TLPLPTLFGN NHMKMDVACK VMLGGKNVED GFGMAFRVLQ
DFQLDAAATY CRAARQLVER EKYSEIRQLL KCVSESGMAA KSDGDTILLN CLEAFKRIPP
QELEGLIQAI HNDDNKVQAY LTCCKLRSAY LIAVKQEHSR ATALVQQVQQ AAKSSGDAVV
QDICTQWLLT SQARGALGSG SRK
//
