ID W5LPH6_ASTMX Unreviewed; 2552 AA.
AC W5LPH6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Zinc finger FYVE domain-containing protein 26 {ECO:0000256|ARBA:ARBA00014373};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000021765.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000021765.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 STRING; 7994.ENSAMXP00000021765; -.
DR Ensembl; ENSAMXT00000021765.2; ENSAMXP00000021765.2; ENSAMXG00000021142.2.
DR eggNOG; KOG1811; Eukaryota.
DR GeneTree; ENSGT00920000149143; -.
DR HOGENOM; CLU_228199_0_0_1; -.
DR InParanoid; W5LPH6; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000021142; Expressed in intestine and 9 other cell types or tissues.
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:0007409; P:axonogenesis; IEA:Ensembl.
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:0048599; P:oocyte development; 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 Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 1820..1879
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 561..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2308..2327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2312..2327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2552 AA; 282849 MW; 414482E278DB60EF CRC64;
MHPFGREQEN SRQDLFGFFT QCLQHGEWEL AAACVQQLGQ AAGDIPQKPS DIITAIVTHP
YPLRWETVGS PHRLAWFWLQ VLEKHSKDKV CESVRRELAF LLLLEELGDE VPVTVLKELH
QAFLDSELVE KKDPHPSVFR LSDAALSCVS SLLSRGRPRL AHALLGFLKD RGLQEVFLQQ
LLERVTAEEQ SEGWAEEVCA MLVLLPCSAG ISGAQLEPLW EGLWRARDGP LSEVKVLGCL
LRPQNQALLT LYCSAVLRLL RARLLQEAPH TQVDLPEAER VTLGLCCHSD RPTVWKVMYF
ECLSSGKHFL EQVLVTGLDL IKKEEFAKLE ALLEVEFQPL SRLLLLLGWK HCQSLDSAQM
LLRILHQQQA QANDTILGEF VNILSSQLGV LEWCVKNNPG ISQEALLSQL RTLDHHSALY
VLHSLTPLAK CEERRVLELL KAAGEPSLGD THNSSVQRNL TLFRGFCAMK YAVYAVCVNA
HTHSGCSSCG LLHIQQKEQA QETQDSEGHS SLFQHYLSEC QLYLETVPAI FRLELLENIF
SLLFLSDGDF NLQTEPCPAA TVTQNSTAAE TEQQTPSSDK LMEDSSVKSE KVADEGRSAG
DHVLPELSHL VSGCRGFLLD ACGMEGVLRL LREGLEGMSA LGQMDGRALG AEAELAESLG
CSVSVDTFSS RLQRLSKRTA EATWRLQIIT SNQGNGAGGP DLPSPGLSST RFLRRSNSSE
VSSVRRKKRS HRHRSEQHVS SERQNGEVSA STSDGGSVAA MCVEQEGCVF GGPHTWLVPA
MLSPPESLLI SCISKGNYME AHQVMLMFGL ENASCSGELL FMERYREVLV ELAQVEQKIE
SQSLSSSSSS EGLGSVGVTV PGRSRLGSSS RSTLQSIGNA AAAGMAFYSI SDVADRLLST
PARPLPCLEE SYWISRPLSD SSLHLLPLLE ELSPAAMAAF DLACCQCQLW KSSRQLLETS
ERRLHASLET RVVRLDPKLL HCEEIHGFPS VLQQISKIVN RTAAGKGPPK SDCNGDDGMV
LAPFGCSAQE VLLCCYPSLT EESIAARLTL TQRLEVTLLT LTSATETAGK SSVSVWVLAS
LLEQAGMKPS ELDSHPVRSA MKQLLRSLDQ LCPFEPDSAT SRPDYMRSFL DYINMLASVL
VRSLGSEDQS LEVKLGNPLL VLLKSPTQLF SHLLFDRQVA PDRVLSLLHQ EGLHVSIQQV
IVQRCCEPLP LFNPYTLKVT GVNGGVFGSA SISSLIKQHA QEHAPTLLDL SDLSDISDTT
PASDPSSESE ISVETNLSTS PPSPSSSSSS SSSSAFLLTQ SALSFLKSRS PLVACLACLS
AARGEVVRPG PSSGWPGLPS YFRSGGRKEA PLDAEQISKE AEALLREFPV LRAFLRDSAQ
PVLGLAEGSD GLGAALCGKA TVGMLFGGPQ GGTGQALAAE AFQQALNGGE LDRALALLEL
YAQSSQQEAL KDRLLACTAL EDRGTEQLFR VKDWQLRGRV ALQGLERWPL QSCLDLLRYC
LSDSSPEEPL TLQLQQKKQE LDMYNKMLSL QPLLEWRTWQ ELKEESSRNP ESMLSLLLQT
REFELCAQWV QLYPVSKQSK LQLQTEHLLY LLEKGRTEEA FQLLESLSEP LALEVSESAL
DRRPGLAACH FLSDYLTLHF QSQMTLARRR HIHALHLGSK VLLTLPEASR QDYFQLLAEP
LLMLEQLLMN LKVDWVSAAV STLRNLLPAQ DAGITNEHID TLLAEYGRKA LDFPYAPRER
SRSDSVISLQ ELSLQCPAQD STPSSPSHTP PPSAGSTPIH TPSSSTYDRE RGSTGKRQRS
LATLFTPPEK MPERKDWIPD HQKHICMVCQ RERFTMFNRR HHCRRCGRLV CHACSTRKMV
VDGYEEPVRV CDQCYNFFHP DSDEELEQAE AGSPVSMDGI LDGVLSLPEV PQKKYRLSPN
PVDNQQINSE FYYEQAPSAS LCVAILTLHS DHAACGHQLI GHCRSISRKL TNPEVDARLL
TDVMQQLMFS AKLMFVRAGR SQDLALCDSY ISKVDVLKIL VSANYKYIPS LDDILETAAI
TRLRNQLLEA EYYRLAVEVS TKSGLDPSGV WHAWGLACLK AGCLSGAREK FSRCLKAPVD
RNQLNMGTRL LQEIVQHLES TVRPTHSTAV DEDILASLAE LEEALRDPAP VERVEGRVQR
CGHYNECLYY LLNYGTHLSL ISFYLRHDGL RDALTHLHNK ECPEDVFLEG VLMPCLERGR
LGALQAQLES LDSSLENWGR YLLSACQLLQ RKGHYHTLFQ LQQFMMDHIR AAMTCIRFFT
HGAHSYLQLG EHQRWLVRAK EHLKTYLQEQ QNRRKPHSTA PSFRKRMSSS DVSRHINTIE
LQLEVTRFLH RCESSSPSKS AISSAPSGNG TPPTLFGASP MKVDVACKVM LGGKNIEEGF
GIAYRVIQDF QLEALAVYER VGQRLVRQRQ YQAIRQLLKC VGESGTATKS DCDAIILSCV
SVAEKIPADA KELEALILES KTAENKIKAY LQCSKLRAAY LLAVKMDVAK AGVLVQDVLQ
AAESSGDSIM QDICRQWLSE HQASRQRHSN NR
//