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VP13A_SCHPO
ID   VP13A_SCHPO             Reviewed;        3011 AA.
AC   P87319; Q9P7M2;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Intermembrane lipid transfer protein vps1301 {ECO:0000305};
DE   AltName: Full=Vacuolar protein sorting-associated protein 13a;
GN   Name=vps1301 {ECO:0000312|PomBase:SPBC21C3.01c};
GN   Synonyms=vps13a {ECO:0000312|PomBase:SPBC21C3.01c};
GN   ORFNames=SPBC21C3.01c {ECO:0000312|PomBase:SPBC21C3.01c},
GN   SPBC31F10.18c {ECO:0000312|PomBase:SPBC21C3.01c};
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Mediates the transfer of lipids between membranes at
CC       organelle contact sites (By similarity). May play a role in
CC       mitochondrial lipid homeostasis, Golgi vesicle transport,
CC       reticulophagy, actin cytoskeleton organization and formation of the
CC       forespore membrane (By similarity). {ECO:0000250|UniProtKB:Q07878}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the VPS13 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB10094.1; -; Genomic_DNA.
DR   PIR; T50345; T50345.
DR   STRING; 4896.SPBC21C3.01c.1; -.
DR   MaxQB; P87319; -.
DR   PaxDb; P87319; -.
DR   PRIDE; P87319; -.
DR   PomBase; SPBC21C3.01c; vps1301.
DR   eggNOG; KOG1809; Eukaryota.
DR   HOGENOM; CLU_000135_0_0_1; -.
DR   InParanoid; P87319; -.
DR   PhylomeDB; P87319; -.
DR   PRO; PR:P87319; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005768; C:endosome; ISO:PomBase.
DR   GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0120013; F:lipid transfer activity; TAS:PomBase.
DR   GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0120014; F:phospholipid transfer activity; ISS:UniProtKB.
DR   GO; GO:0120009; P:intermembrane lipid transfer; ISS:UniProtKB.
DR   GO; GO:0045324; P:late endosome to vacuole transport; ISO:PomBase.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0045053; P:protein retention in Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; IBA:GO_Central.
DR   InterPro; IPR026847; VPS13.
DR   InterPro; IPR026854; VPS13-like_N.
DR   InterPro; IPR031645; VPS13_C.
DR   InterPro; IPR017148; VPS13_fungi.
DR   InterPro; IPR031642; VPS13_mid_rpt.
DR   InterPro; IPR031646; VPS13_N2.
DR   InterPro; IPR009543; VPS13_VAB.
DR   PANTHER; PTHR16166; PTHR16166; 1.
DR   Pfam; PF12624; Chorein_N; 1.
DR   Pfam; PF06650; SHR-BD; 1.
DR   Pfam; PF16908; VPS13; 1.
DR   Pfam; PF16909; VPS13_C; 1.
DR   Pfam; PF16910; VPS13_mid_rpt; 1.
DR   PIRSF; PIRSF037235; VPS13_fungi; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus; Lipid transport; Reference proteome; Transport.
FT   CHAIN           1..3011
FT                   /note="Intermembrane lipid transfer protein vps1301"
FT                   /id="PRO_0000116877"
FT   DOMAIN          2..115
FT                   /note="Chorein N-terminal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          2143..2415
FT                   /note="SHR-BD"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   3011 AA;  346899 MW;  8EE431CD9AA42018 CRC64;
     MLEGLVAGLL NKILGSYVDN LDTKQLNIGV WGGHVSLHNL RIKPEALDKL GIPIEITSGL
     IGTFTLEIPW SNLRNKSLTI NIEDIYLSIH PQAKNSLTRD ELEQSQQALK QEQLDSFEIL
     RKNFRETLEE SSSNPNISRK QSFIEYLIAK LTDNIQIYIE RIHLRFEDNL SDLEKPYSLG
     LTLYSLRVTS TDASFTEYLL STDPIPSSCI HKIITVDYFS IYWISKCEIS KCTTTEDIFS
     YLKNLIPSAE KSPAYNYILK PLRATAHVVL FRHPTDQIMQ LRGKLSVEEI SITLSDHMYY
     SLLGVIDYFR VVMKQQYYLQ YRPKSTPKEK PLEWFKYAIL VVKDSVHESR YHWTWKYFKR
     RRDDRIAYMH IIRKRYLNEQ ISKEEIDLQK KIEKRNSTYD LIKYRSRVHT SLIEERNSIY
     LKPKTSAAHG LYDWFSGYIR KPQSQDEDTL ASTDKTAADL TDQEQKEFFS AIEWSGQLYP
     DTVNLDPDMC MANVEVSIAK GSFVIQSHIN GRVIPLIKQR FESFATECFI RPQSLKLKVS
     LKDLDMFDGI TNPELEPARV IFAKPSVEES ESLQKIPEAY RTHLFFLLLD TKPVYKASST
     LIVHLRTLVI IYNRVCIESL LAFFVPPRTK IEHVSEWGYS AAAKVMTLAR QTRASLDYAL
     EMHKTSDMTI DLQAPLIVVR EECTDLKSPT LFLDVGRALV HTQLVDDAII DKFRKLQSKK
     INNEQLKQLE NLMYDKFTIS LFNVRCLIGP DYETGWRCLP KGCDYHILKE CSLDINFEIS
     ILQKATNLTK FKVSSHMKHA EIMFSDVQYK VFINMMSNIL PTLPVAEIPF TYQQFLDAVK
     PPPFFDAPDN FQITHTSLGS HANENTAAQF MAQQIFAFYF KVDYAICSLY RRSENYLIPV
     VRAFTEFYID LVVRKFDYLV TSKLNDLVIK EFTYPSSLCD NVLVRSSPSP KNNFDDTVFI
     SYTSIDYDSP ELDSVYEGVR TTIAVVLSDL ILNVEPTGFS FVYDFIRATF TSLNDEYMIG
     EDPELTRKIS PVEGIIPEDA NVRFDNVDIF LYDCDQHFST VCLYSANMHM EFREKFFLQA
     RFYDLEVKNH MKSNNPPKTI VKIDDNDLFI FKYESYDIPK DISKPTCDCV YDISFGSLTF
     YFQKSYFNAI YDFLLKLKRF QELFSSIRYA IYYKLYGNKV SLTYPKFELR IKHPKVYFDD
     VLDEERNCRM QLIVKPQSFY AFSKCPIVEK NSKKSIFSCE ITKVEFHTAV PSSSHHDVLM
     EENNVHLDLT YDANYTTGAY VFKATGDLDP VILNMCQSHH VIFWDLIDVA TTFARVDSSF
     YTSENLRREL DKAFDRSGTA AKLKHPKKTV VETLDILTTF NLPEIRLNVH TDDFWIHGGD
     LTQLHSILSF FGFSLDYNFY SSGRCYAEFS IDSIQLKDCN PQDNVVFLDV LEYSENHNRL
     VNGCLEYDSQ NPRYNLVLDI DSPKIFVNLN YLYSIWSIFV HWHRAYYSHL DYLTEVEYFI
     MGNPNQNACG EESYWYYRIT FVDMTLLFFR NVSDANLYSL PMFFGELLIT QQSIFAVTAN
     NMKINACPLS ETANISNQLA DPFGFRYTYS QHTVNKIQII TNITLDFDSF VLRTTVNDFL
     FLQTILRKIY NFYYALYDVP TTDVELLKRT KDDQLATNPD FLQLSVDTGQ PSSVFGIRIC
     KEEFLLTVDG IRLLVISQLH DLPLLNINIK PFQVDLNDWS SELNSNAHLE LFMNFYNFSN
     SHWEPFLEPW KVGVHISRNP NTSKTAVHVF SREKLDLVIT PQLIETLHFG FTKVISTPFP
     IEFKCDAPYR IHNYTGHAVS VWADFENAAD SCVRHLENNE ETDWKFEEWR QMQDVVKQDQ
     DRSYIGFHFE NSKWESLRHV RVNRVGEHIY PLISYDQDEL KHYMVVDVNL GEDYIKHITL
     RSPLLLINET QMEIDVVFCD SDGIQRSQIY HMSPEESCSL PIETAYYYSI HIRPVSEFKF
     NWTSEAISWK DLVDNKQSLV TCQHSDNTFS TPACRFAANA ELKSQTISNH YPFMHITISA
     LLEVKNLLPI DLNIRIIDKD QEGVWMSNVG IGECAYVHSI NISHVLLLQA ESSESHYLPS
     SLATIITNDS AQERDEYMTI TLQGGRKTRL GLSYTEKYPG IYHIEIFSPY IIINKSGSFL
     FVGPKNDYNR ISFSSASLSS GEDGKVVPCM FSYSHNYGSR RCRLRADNSN WSEPVSFDAI
     GSVFEVELPS KEDHNKVYRL GIFVETGPDG YSKTNIVTIT SRFIVRNKTR WSLVIAEPYN
     DFIAEIAPEG EEFLTYLRKH SHPMLKLSSS DCYLWSSSFY IEEIGSTHVR LMTSEGEKLL
     RLEIVIKNAT IFISIFEETG DWPYYIKNES GVLLKFWQVN PIDASEGKNN TALLKYHDIP
     PHSEVKYSWD YPCCANKEIA LCYGDQKCLT TLAEIGPLSP FKFTDASNNT KFISRDIVAN
     GLSKILILKD YDPSKAVRKP KIYSKVSTEE RDFNLEQFDS GIDLSVKFLL EGIGISLVER
     NTQELAYLTF HGINLFFTDS HLIRTFKLDV RWIQIDNQLY GGIYPIILYP SILSQEDTMN
     DNSLLPTFHS MVAVVKNDTY GVTYVKYATI LLQELTIEID EDFAFAALEY IKDSVPRSKR
     NTGKMFDDSL ELVPENLGND LKVYFEVLNL QPTEMHLSFV RTERINNTDG TVVSSHNPFV
     FFVNVLSMAI GNINDAPVRL NALLMDNAHV SLRRLFELVK NHYSQELLSQ VHKIVGSADF
     LGNPVGLFTT ITSGFADIFY EPFHGFILNE GSYELGIGFA KGTASFIKKA VFGITDSISK
     VTGTISRSLS VITLDPKFQS RRRAARIRNR PVHILYGVTA GAASLYTGVR SGVRGLALQP
     IIGARRNGLP GLVKGLGKGL VGFTTKPLVG LFDFASSISE GARNTTTVFD ERHIEKLRLS
     RLMSDDGVVY PFQLREALGQ YWLKHLDNGR YFKDFYKAHI IIENKVLVIL TNNRILFVQP
     QQLNCKKEIH L
 
 
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