YKH3_SCHPO
ID YKH3_SCHPO Reviewed; 1225 AA.
AC Q9UT00; Q9UTV4;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Uncharacterized protein PYUK71.03c;
GN ORFNames=SPAPYUK71.03c;
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 928-1115, 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-843, 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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}; Single-pass
CC membrane protein {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB52146.1; -; Genomic_DNA.
DR EMBL; AB027973; BAA87277.1; -; Genomic_DNA.
DR PIR; T39255; T39255.
DR RefSeq; NP_593974.1; NM_001019400.2.
DR AlphaFoldDB; Q9UT00; -.
DR SMR; Q9UT00; -.
DR BioGRID; 278736; 20.
DR STRING; 4896.SPAPYUK71.03c.1; -.
DR iPTMnet; Q9UT00; -.
DR MaxQB; Q9UT00; -.
DR PaxDb; Q9UT00; -.
DR PRIDE; Q9UT00; -.
DR EnsemblFungi; SPAPYUK71.03c.1; SPAPYUK71.03c.1:pep; SPAPYUK71.03c.
DR GeneID; 2542267; -.
DR KEGG; spo:SPAPYUK71.03c; -.
DR PomBase; SPAPYUK71.03c; -.
DR VEuPathDB; FungiDB:SPAPYUK71.03c; -.
DR eggNOG; KOG1012; Eukaryota.
DR HOGENOM; CLU_001661_1_0_1; -.
DR InParanoid; Q9UT00; -.
DR OMA; YMPVLSQ; -.
DR PhylomeDB; Q9UT00; -.
DR PRO; PR:Q9UT00; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031520; C:plasma membrane of cell tip; EXP:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; ISM:PomBase.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IC:PomBase.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; ISO:PomBase.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd04044; C2A_Tricalbin-like; 1.
DR CDD; cd04052; C2B_Tricalbin-like; 1.
DR CDD; cd04045; C2C_Tricalbin-like; 1.
DR CDD; cd04040; C2D_Tricalbin-like; 1.
DR Gene3D; 2.60.40.150; -; 4.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037761; C2A_Tricalbin.
DR InterPro; IPR037765; C2B_Tricalbin.
DR InterPro; IPR037762; C2C_Tricalbin.
DR InterPro; IPR037756; C2D_Tricalbin.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR017147; Tricalbin.
DR Pfam; PF00168; C2; 4.
DR PIRSF; PIRSF037232; Tricalbin; 1.
DR SMART; SM00239; C2; 4.
DR SUPFAM; SSF49562; SSF49562; 4.
DR PROSITE; PS50004; C2; 4.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Calcium; Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1225
FT /note="Uncharacterized protein PYUK71.03c"
FT /id="PRO_0000116827"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 217..422
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 413..534
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 559..668
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 685..803
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1019..1137
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1053
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1053
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1059
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1225 AA; 135781 MW; 7041FCAA5A6D7B96 CRC64;
MSSQAEPSKG ASNADPNEKV EKMHLPTDTA GGGVKVKVKE QEASPSDKNN LNPQSAGVSE
VQVQDDTGAR GSGARDLKVP KQMQAPKSSE EKSDVDGVPT RPVSERELRK RDAMQFIQRH
QKVRNILAQY CPWLTDERLQ LCIELKILFM QHFQDSRLVL YTAVMSFLFG YLRFGFLSLF
IIMAVCIQYY RICDRRVKVN FKDDYTRYLS TRKLENDSET VTWLNTFLQQ FWYIFEPSLS
ERITEITDQI LSENVPSFID SMALSEFTLG TKSPRMGFIR SYPKTEEDTV MMDLRLAFSP
NDISDLTGRE IAACIKPKIA LDLKIGKSIA SAKMPVLIED LSFTGNLRVK VKLIDKYPYA
KTVGLTFTEK PVFSYILKPL GGDKFGFDIG NIPGLTTFIT EQIHNTLGPM MYSPNVYELD
IESMMGAAGL NTALGAVEFK LRKGDGFKDG LGGAVDPYVV IKNSADRVIG KSKVAHNTGS
PVFNETFYSV LNSFSENLNL EVYDFNDIRS DKLLGSAVLP LATLEAMPVT NDAFVELTLK
GKTVGRLNYD MKFHAVVPDS GEEITKVDGP GVLQFTVHQC KELSNDPSKR PTAYAKLIIN
NKEVYTTRKI KKNNNPSWEE SFGTLLPEGK NATLGVQIFT EESEHPFGTA NVSLQDLFAA
TKTGLLWFPL QHAPSGRVRM SVMWKPAQLN NDSISSMALA TPIGAIRIHL RSANNLHSKI
PGKKCDSYAR IMSHNTKQFR TVVIASNVNP FWDEYMYAPV ITKHDIFFLQ VMNYNSSGED
KLIGQTPINI SNFINQGENG ALMEYHDPRE LTVPLSSTRG IKGNATITFK CDFFPSAVTT
SLSPDVTPAP KASSTVATDK VNIEVLPESQ KTPTAVDNTS TSRGSTSVKT SKPKKISELL
MPSEAVNAAL DFESGFMGFD IISYKIAKPA QELAIFLDDL PHHIFLSSAL NVTGGATLHE
YGNTFIRQLE YSQCTFKLLD GDKEVGSKTM LSRDLISKGA TKPLEIAFPD GASILVAFRL
TPVPVKLEEV EMYENMGEMT VDVIKATDLP AADSNGKSDP FVVFELQGEE VYRTKTHKRT
LNPTFNESFE VELPCKQTCN FVANVFDWDF GNKDDHLGSC VIDCKLLQQQ QQTNYEIPLD
SKQGVLYLRI TLSPKWVLRS KRAGNSSLVE GILGQTASIV GMPLKGISTV GNVAVDGVAS
VANLTNKMRK GISRGFKGIH HEKAK