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YF2E_SCHPO
ID   YF2E_SCHPO              Reviewed;         617 AA.
AC   O13779; O13763;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 4.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Putative metal ion transporter C17A12.14;
GN   ORFNames=SPAC17A2.14, SPAC17G6.01;
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   INTERACTION WITH SAD1.
RX   PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA   Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT   "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT   membrane-bound components of the spindle pole body in fission yeast.";
RL   Mol. Genet. Genomics 270:449-461(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-152; SER-162;
RP   SER-226 AND SER-241, AND IDENTIFICATION BY 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   -!- SUBUNIT: Interacts with sad1. {ECO:0000269|PubMed:14655046}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC       family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16566.1; -; Genomic_DNA.
DR   PIR; T37815; T37815.
DR   PIR; T37833; T37833.
DR   RefSeq; XP_001713086.1; XM_001713034.2.
DR   AlphaFoldDB; O13779; -.
DR   SMR; O13779; -.
DR   BioGRID; 858055; 10.
DR   IntAct; O13779; 1.
DR   STRING; 4896.SPAC17A2.14.1; -.
DR   iPTMnet; O13779; -.
DR   SwissPalm; O13779; -.
DR   MaxQB; O13779; -.
DR   PaxDb; O13779; -.
DR   PRIDE; O13779; -.
DR   EnsemblFungi; SPAC17A2.14.1; SPAC17A2.14.1:pep; SPAC17A2.14.
DR   PomBase; SPAC17A2.14; -.
DR   VEuPathDB; FungiDB:SPAC17A2.14; -.
DR   eggNOG; ENOG502QPTQ; Eukaryota.
DR   HOGENOM; CLU_413973_0_0_1; -.
DR   InParanoid; O13779; -.
DR   OMA; SHEMWEL; -.
DR   PhylomeDB; O13779; -.
DR   PRO; PR:O13779; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0015095; F:magnesium ion transmembrane transporter activity; IMP:PomBase.
DR   GO; GO:0010961; P:cellular magnesium ion homeostasis; IBA:GO_Central.
DR   GO; GO:1903830; P:magnesium ion transmembrane transport; IMP:PomBase.
DR   CDD; cd12829; Alr1p-like; 1.
DR   InterPro; IPR044089; Alr1-like.
DR   InterPro; IPR045861; CorA_cytoplasmic_dom.
DR   InterPro; IPR045863; CorA_TM1_TM2.
DR   InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR   Pfam; PF01544; CorA; 1.
DR   SUPFAM; SSF143865; SSF143865; 1.
DR   SUPFAM; SSF144083; SSF144083; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..617
FT                   /note="Putative metal ion transporter C17A12.14"
FT                   /id="PRO_0000201538"
FT   TRANSMEM        560..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        590..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   617 AA;  71198 MW;  99BA5F8A5E691249 CRC64;
     MPSNTSRSVP TGFYYKQNAR MQNRPRFSDR KHSSKSKHRF PVDPSLQPDE ADEGTRLLGN
     SDSDLLEPPS EHSSNGEDDK DINNPPSMPS SVCSSPKSPH RHYESDEDIE NISLPESHPE
     DIQRKEFETE NGKNTRDQPS PLAEVSDFAI SSPHVYPKSA NSHDSHYEQF ANNDVTESAV
     DDHPATRKLS RDELYLPISP NNAQEPKFSV LDEWTKKMVA NFEEYSVEDV DKRRERNRKL
     SEPLLVNGRY RVRDRWAQFR KSEIEKPYRF TFFTDELPST IHSHEMWELV HDGQSFEDLF
     HSGGTWWLDV SCPKEEEIRV LAKAFGIHPL TVEDITLEED REKVELFRTY YFVTFRSFNQ
     LPSNSEYLKP LNFYLVVFRD GIITFHMNPT PHPANVRRRI RQLNGYLTVN ADWIAYALLD
     DTTDAFAPFI EQIEDEVDTI DSMILSIHYD HVMEVKPQER MLQRVGECRK LIMSLLRLLA
     NKADVVRGLS KRCNESWQVA PRGEIALYLG DVQDHIVTMV QNLNHYEKIL SRSHSNYLAQ
     ISINMTLVSN ETNEVLSRLT ILGTILIPLN LVTGLWGMNV KVPGQDVPGL GWFFSILGSL
     MIFAISSFIL CKWYKVI
 
 
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