YGZ7_SCHPO
ID YGZ7_SCHPO Reviewed; 764 AA.
AC O42976; Q9USA4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Uncharacterized membrane protein C20F10.07;
GN ORFNames=SPBC20F10.07;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 515-729, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Note=Localizes to cytoplasmic punctate
CC structures. {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the YSP2 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA16847.1; -; Genomic_DNA.
DR EMBL; AB027914; BAA87218.1; -; Genomic_DNA.
DR PIR; T39878; T39878.
DR RefSeq; NP_596371.1; NM_001022292.2.
DR AlphaFoldDB; O42976; -.
DR SMR; O42976; -.
DR BioGRID; 277227; 11.
DR STRING; 4896.SPBC20F10.07.1; -.
DR iPTMnet; O42976; -.
DR MaxQB; O42976; -.
DR PaxDb; O42976; -.
DR PRIDE; O42976; -.
DR EnsemblFungi; SPBC20F10.07.1; SPBC20F10.07.1:pep; SPBC20F10.07.
DR GeneID; 2540703; -.
DR KEGG; spo:SPBC20F10.07; -.
DR PomBase; SPBC20F10.07; -.
DR VEuPathDB; FungiDB:SPBC20F10.07; -.
DR eggNOG; KOG1032; Eukaryota.
DR HOGENOM; CLU_375149_0_0_1; -.
DR InParanoid; O42976; -.
DR OMA; YIKPVAP; -.
DR PhylomeDB; O42976; -.
DR PRO; PR:O42976; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0140268; C:endoplasmic reticulum-plasma membrane contact site; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0071561; C:nucleus-vacuole junction; ISO:PomBase.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; ISO:PomBase.
DR GO; GO:0008289; F:lipid binding; EXP:PomBase.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; IMP:PomBase.
DR GO; GO:0120011; P:intermembrane sterol transfer; IC:PomBase.
DR GO; GO:0032366; P:intracellular sterol transport; IBA:GO_Central.
DR GO; GO:0015918; P:sterol transport; EXP:PomBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR031968; VASt.
DR InterPro; IPR040147; Ysp2/Lam4-like.
DR PANTHER; PTHR23319:SF4; PTHR23319:SF4; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00568; GRAM; 1.
DR PROSITE; PS51778; VAST; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..764
FT /note="Uncharacterized membrane protein C20F10.07"
FT /id="PRO_0000374037"
FT TOPO_DOM 1..646
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 197..264
FT /note="GRAM"
FT DOMAIN 432..598
FT /note="VASt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01114"
FT REGION 22..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 764 AA; 85355 MW; 080990E5C7F4A7B2 CRC64;
MKEENGFAGF LNTAVNRLSG VLNDTAPTKS QSLKNGVNNE GNRGFSLFRN PRFMSDEKLS
SEASSHSTLG QQQARDGRQS PSKEAPFGEG ELKLENFENQ ENEADEAENE ETSYSEQNHT
ENTEEIAEES RPLERTHSGS NHHEASSTGH LNLPPLENTL SQGSAITAPS RKVSITSSNG
VSARLSGYAF ANSKRNRDFH RIFKVLPPED HLIDDYGCAL QRDIFLHGRM YLSESHICFN
SSIFGWVTNI VIPVTEIVSV EKKSTAVVFP NAIQITTLHA RYIFASFISR DTTYQLIIAI
WKNTHPFLTT LANGHGVMDA SGNHHSGSSN QSINADSSAG SEGVDEGTST EANDESSEDD
DEDNNTDEAN EDAQSNVSDE SPKGEGSSHS DNVVLSDGNS VKKMNEDGAD TSLLSVSEVT
SHPPTEWTGS PLAHVLCSDV VNLSVSTVFN LLCGSDTTWI INFFKSEKLT EIKIGKWEKI
DDKWNRKVQY IKPVAPPYRQ TSCYITDTIQ HLDINNYIEI LSTTSTPDVP SGTSFVVKTL
YALSWAHSSK TKLNISYSVE WSKSSWLKGP IEKGAQEGQA SYVKDLLTAF ENYKVSPKGR
RKKITKHTKK KNKHASETSV APEKVDNSSI EQSSSFLTKL YTFPFTIITW LMHPTHLLLV
VMFSMLVLQW WYMQQILHAE LPSTSSRSDS SRDLDFDHIP MDDTAFKLWI TSRLDSVERD
RDFVYENSDP NLEHGKIKIA TDYMERRLKK LKERLRKLEA SGYI
