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VPS27_NEUCR
ID   VPS27_NEUCR             Reviewed;         724 AA.
AC   Q7RZJ2; Q870P0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Vacuolar protein sorting-associated protein 27;
GN   Name=vps27; ORFNames=49D12.130, NCU04015;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Component of the ESCRT-0 complex which is the sorting
CC       receptor for ubiquitinated cargo proteins at the multivesicular body
CC       (MVB) and recruits ESCRT-I to the MVB outer membrane. {ECO:0000250}.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of hse1 and vps27.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- DOMAIN: The FYVE domain is involved in the binding to
CC       phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the
CC       association to endosomal membranes.
CC   -!- DOMAIN: Both IUM domains are necessary for efficient binding to
CC       ubiquitin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS27 family. {ECO:0000305}.
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DR   EMBL; BX295540; CAD79688.1; -; Genomic_DNA.
DR   EMBL; CM002241; EAA28394.3; -; Genomic_DNA.
DR   RefSeq; XP_957630.3; XM_952537.3.
DR   AlphaFoldDB; Q7RZJ2; -.
DR   SMR; Q7RZJ2; -.
DR   STRING; 367110.Q7RZJ2; -.
DR   EnsemblFungi; EAA28394; EAA28394; NCU04015.
DR   GeneID; 3873817; -.
DR   KEGG; ncr:NCU04015; -.
DR   VEuPathDB; FungiDB:NCU04015; -.
DR   HOGENOM; CLU_011862_1_0_1; -.
DR   InParanoid; Q7RZJ2; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033565; C:ESCRT-0 complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR   GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR017073; HGS/VPS27.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR002014; VHS_dom.
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   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF02809; UIM; 2.
DR   Pfam; PF00790; VHS; 1.
DR   PIRSF; PIRSF036956; Hrs_Vps27; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00726; UIM; 2.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; SSF48464; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS50179; VHS; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   3: Inferred from homology;
KW   Endosome; Membrane; Metal-binding; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..724
FT                   /note="Vacuolar protein sorting-associated protein 27"
FT                   /id="PRO_0000292520"
FT   DOMAIN          18..150
FT                   /note="VHS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT   DOMAIN          270..289
FT                   /note="UIM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   DOMAIN          317..336
FT                   /note="UIM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT   ZN_FING         168..228
FT                   /note="FYVE-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          228..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..257
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  79747 MW;  A66FBF68B32CC1DD CRC64;
     MMSWWSSGAN TALDEQIEKA TSSSLEDIAL NLEISDVIRS KTVQPKEAMR SLKKRINHKN
     PNTQLSALNL TDTCVKNGGA HFLAEIASRE FMENLVGLLK AVGPAAPNPD VRNKILDLIQ
     SWAMAAEGRY ELSYIGEVYK TLQREGYSFP PKPTVASSMI DSSAPPEWVD SDVCMRCRTA
     FTFTNRKHHC RNCGNCFDQQ CSSKSLPLPH LGIMQAVRVD DGCYAKLTDK GGKSGGSDRK
     HHSSSRHHHH HHKHKSSSSM QPRDARVDDS FDEDLKRALA MSLEEVKSYS RGHSEPANST
     QYKPDKQSTS VSKIAEEEDE DLKAAIAASL ADMEEQKKRH AAALKEQTSN VGSSSSAAPF
     TLPKNDYELT PVEAENINLF ATLVDRLQTQ PPGTILREPQ IQELYDSIGA LRPKLARTYG
     ETMSKHDTLL DLHAKLSTVV RYYDRMLEER LSKAYGQHSI GGYNLPAPRQ PTGPYPTLDP
     SAPSAPGAAE NFYTGEQQAD YSHAPYGQYP PQPPQSQYMP YDRRSSMVGP PNPQYPQQQM
     PQRTGSWGNA PPAQAPQYNY SGNEVAPSQP GHAQQAQPGA PESAPGAPNN DPNASYYYNP
     GQPQQQQQQS AQQAPAAAPD HSYPTLPQQG HSYQPSVPQT PASVPVQPSQ TPQQAHQRVP
     PPQQAPQQPY WQHSAAQQTP LPPVWQAPQQ TTTYPGYDQE AFPSAPQHAP APKQPVVEEA
     LIEL
 
 
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