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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}.
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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
 
 
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