VPS91_SCHPO
ID VPS91_SCHPO Reviewed; 572 AA.
AC O74396; D2CFN6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Vacuolar protein sorting-associated protein 9a;
DE AltName: Full=Vacuolar protein-targeting protein 9a;
GN Name=vps901; Synonyms=vps9a; ORFNames=SPBC4F6.10;
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 [MRNA].
RA Miyamoto M., Saito N., Matsuda T.;
RT "Schizosaccharomyces pombe Vps9 protein mRNA, complete cds.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
RN [3]
RP IDENTIFICATION OF FRAMESHIFT.
RC STRAIN=972 / ATCC 24843, and JY3;
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP REVISION OF GENE MODEL, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21270388; DOI=10.1534/genetics.110.123497;
RA Bitton D.A., Wood V., Scutt P.J., Grallert A., Yates T., Smith D.L.,
RA Hagan I.M., Miller C.J.;
RT "Augmented annotation of the Schizosaccharomyces pombe genome reveals
RT additional genes required for growth and viability.";
RL Genetics 187:1207-1217(2011).
CC -!- FUNCTION: Required for vacuolar protein sorting; may be required for
CC the consumption of transport vesicles containing vacuolar protein
CC precursors. {ECO:0000250}.
CC -!- DOMAIN: The CUE domain (Coupling of ubiquitin conjugation to ER
CC degradation) is monoubiquitin-binding and is required for
CC intramolecular ubiquitination. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20730.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ665299; ABG66956.1; -; mRNA.
DR EMBL; CU329671; CAA20730.2; ALT_FRAME; Genomic_DNA.
DR PIR; T40507; T40507.
DR RefSeq; NP_596110.2; NM_001022027.2.
DR AlphaFoldDB; O74396; -.
DR SMR; O74396; -.
DR STRING; 4896.SPBC4F6.10.1; -.
DR iPTMnet; O74396; -.
DR MaxQB; O74396; -.
DR PaxDb; O74396; -.
DR PRIDE; O74396; -.
DR GeneID; 2540886; -.
DR KEGG; spo:SPBC4F6.10; -.
DR PomBase; SPBC4F6.10; vps901.
DR eggNOG; KOG2319; Eukaryota.
DR HOGENOM; CLU_007625_3_3_1; -.
DR InParanoid; O74396; -.
DR PRO; PR:O74396; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; ISO:PomBase.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:PomBase.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:PomBase.
DR Gene3D; 1.20.1050.80; -; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR041545; DUF5601.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF02845; CUE; 1.
DR Pfam; PF18151; DUF5601; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00546; CUE; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..572
FT /note="Vacuolar protein sorting-associated protein 9a"
FT /id="PRO_0000316571"
FT DOMAIN 219..357
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT DOMAIN 529..571
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 65554 MW; 1F617712EF331CF1 CRC64;
MDYPSFHEDP TKDESTVAEQ RKGQSNEEKP LIDLNDSLDE QRNAYNEHCK NHDQQPSQQV
RNMEDEANQY EQTDSSSDQE VMNEKQSLDK ENRNDNIPHE NNPGQQEINE PIFDFHMFLE
QLRSSSAEPV AKYLKSFLSE FTKRRWTVNY QVKLIRDFLK FINEKIEQYE PWASGSQAEI
DNAKEGMEKL VLNRLYTSLF SPEIAKSGIP LSSEHSDDVE EDRVLSEKME LFQWITEENL
DIKKQKSSSK FFKLAADELR RINDYHAPRD KIICLLNCCK VIFSYLRNVV KEESADMFVP
ILIFVVLQAR PAHLVSNIQY IQRFRSPEKL TGEVMYYLST LMGAMSFIET LDCSSLTITE
EEFNAQIEKS IKKMEERKLS EKSESKTAVN ENATYKDPVL SRGLSSSIDV STGVALVNLP
EELENMKYLQ IDTPESKEYP RSTRPRASSH SGSFTTDSGK RSRRNSNKYV GSSDRPPYRV
SRAYSSSATH SPIVHEEQPV DDGLQQNDDL REATTASLET AEAERLQARE KAEAITALRA
MFPAFDSEVI EVVLNAQQGR LSSSIDSLLE MS
