ID Q4RH19_TETNG Unreviewed; 1960 AA.
AC Q4RH19;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Zinc finger FYVE domain-containing protein 26 {ECO:0000256|ARBA:ARBA00014373};
GN ORFNames=GSTENG00034557001 {ECO:0000313|EMBL:CAG12313.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG12313.1};
RN [1] {ECO:0000313|EMBL:CAG12313.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|EMBL:CAG12313.1}
RP NUCLEOTIDE SEQUENCE.
RG Genoscope;
RG Whitehead Institute Centre for Genome Research;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CAG12313.1}.
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DR EMBL; CAAE01015073; CAG12313.1; -; Genomic_DNA.
DR KEGG; tng:GSTEN00034557G001; -.
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; 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 1168..1228
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1711..1730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1895..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1943..1960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1960 AA; 215672 MW; 6317740DBE9AD1DD CRC64;
MDSGAGCSQR QRRARVPAAS GGAGVRGHNR ECYQEEPESS PGPGVQKNIV LFQGFCAMKY
AIYALFVNAH KGFLVDVTAV EGFLKLLKDG LEGMSVTDQQ EGQEPGRAFH QEAEGAERIG
CSVRPETFGT RLQRLSKHIA EAQWRLLIIT SNQGGGSGLE SPVQVSQMFD LEKSACSGEL
MFMECYKEVL VELERVEQKM ENQSLSSSSS SSEGLGMAAV SGTGRSRVGS SGRSTLQAIG
SAAAAEELSP AAMAAFDLAC CHCHLWKTSR QLLDTAERRL SSSLEARGVK VNPMVPNLEG
IRGFPMVLQQ ITKILNHSST YKSSVKTDSV GEDLAFASPF GCCIQEVLLC CHPVLSEECI
AARLGLVQRL ETALHVLSTA TDGADSSVGS ALPALLVEQA SLKQSELDAH PVRSNIKQLL
RTLDQLCPFE PDGGLARPDY MRSFFDYINT LASVVVRSLG SEEQSSEVKL GNPLLVLLQP
PFQLFSYLLF DRQVSPERLL LLMQQEQLHL SVQEVIIQRC CKTLPVWTFS PDGDRKTDST
QDKKDPGVFS TASLSVLLQQ HAQEHLSTLG ITESQSDSSS ESEASAEERS ATPTSLSTSP
NSSQSLSSSS SNTFLLTPSA LSFLKSHSPL LATLACLSAC KGEAGRAQSS GWSGYFRSGR
REVVLEVEHI AREADHLLKG FPILWDYLHS MAEPVLGTLS SEDEEESPGL GAAVCGKPLI
SLLLSGPQEE VAQVVAAEAF QKALSSRDLG RALRLLELYG QGCSQEGVLR DQLLACAALQ
DGGGSIAQLF RVQNANLRAR VALQALEKWP LSACRELLEF CLNDLGTESS LRTDLEVKKK
ELDIYHRMLT LNPPLPWATW QELRSESQLN SETVLSKMLE AKEFSLCAQW AEVYTVPDQL
RLQLKTEHLL HLLEEEQADE AFQVLHSLTA ASLEQQRPCT DKSLVLQLLE GLSDSVVGLD
ICERALDRRP GLAACHFLAD YLTLHFQRQV SPARRRHIHA LHLGSKVLLT LPPAARQDYF
SLLSEPLLML EQLLMNLKVD WADVAVRTLR SLLVGQEAGF TSSDIDKLLE TYASKALHFS
CAPSERSRSD SVISLQDSLL MCPAQDTSSQ SSGRVDSPSP STGDTPTHTP SSNSSDKEKD
RVLGKKRLST AKFQPPERPP AYKDWVSDDK HHVCMVCQRE KFSMFNRRHH CRRCGRLVCQ
ACSERKMLVE GFREGGVRVC DQCYDFFHPA ADEEDEPNEV SGSPLVTGDA LDGMLYLPDV
VQMQIQLSSN AAENQLLRSE FYYEQAPSSH LCVSILSLHS DQAACGHQLI EHCRALSRRL
TNPEVDACLL TDVMQQLLFS AKMMFVKVGR SQDLALCDSY ISKVGVLKIL VKANYKYIPS
LDDILETSAV TCLRNQLLEA EYYQLAVEVS TKSGLDPSGV WQAWGMASLV AGNLSGAREK
LARCLKPPMD RNQLNLGSLL LQEVIRHLEN DVPPTLSMFQ SSDEDILASL RDLEAVLQES
PLDRPEGQSL SSDLQQECLY YLNTYGTHLA LISFYMRHDC MTEALTYLLK RECPEEVFLE
GLLQPCLERG RLSALQGMLE KLDPTLEACS RYLIASCQFL QRRRYFNTLY QLQQFMMDHV
RAAMTCIRFF THGASSYLQL GEQQRWLVRA KDHLKTYLQE QQGRSGGRRR SQVNSFRKTM
SSSDVSRHMN TIELQLEVTR FLHRCEGAAS SSSLQTSAPP SKSVGSSSPP TLFGGSAMKV
EVACKVMLGG KNIEEGFGIA YRVIQDFQLE AQVVYTRAGQ RLVRQRQYGA VRQLLKCVGE
SGTATKNDCD ALILSYISVA DKAPADVRDG SSRSTNTLIQ TNLYLRFVSF PLSRPKNWIV
SFWRPKALKT SESELIRRLR VPADQSLPAL QQTATGLPAS GEAGGEPGQP AGPRCPSGRR
GSSGLGDAEH LPPVAGGTQR LVSAAPGSAQ RQVKAQPSLL
//
