YNSG_SCHPO
ID YNSG_SCHPO Reviewed; 1050 AA.
AC O60146;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Uncharacterized transporter C18H10.16;
GN ORFNames=SPBC18H10.16;
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] {ECO:0000312|EMBL:CAA18413.2}
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-60; THR-64; SER-270;
RP THR-271; SER-901; SER-936 AND THR-939, AND IDENTIFICATION BY MASS
RP 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:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SLC12A transporter family. {ECO:0000255}.
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DR EMBL; CU329671; CAA18413.2; -; Genomic_DNA.
DR PIR; T39780; T39780.
DR RefSeq; NP_595740.1; NM_001021638.2.
DR AlphaFoldDB; O60146; -.
DR SMR; O60146; -.
DR BioGRID; 277348; 10.
DR STRING; 4896.SPBC18H10.16.1; -.
DR iPTMnet; O60146; -.
DR MaxQB; O60146; -.
DR PaxDb; O60146; -.
DR PRIDE; O60146; -.
DR EnsemblFungi; SPBC18H10.16.1; SPBC18H10.16.1:pep; SPBC18H10.16.
DR PomBase; SPBC18H10.16; -.
DR VEuPathDB; FungiDB:SPBC18H10.16; -.
DR eggNOG; KOG1288; Eukaryota.
DR HOGENOM; CLU_001883_4_0_1; -.
DR InParanoid; O60146; -.
DR OMA; VHSNSMT; -.
DR PhylomeDB; O60146; -.
DR Reactome; R-SPO-426117; Cation-coupled Chloride cotransporters.
DR PRO; PR:O60146; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0031166; C:integral component of vacuolar membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; NAS:PomBase.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IBA:GO_Central.
DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central.
DR GO; GO:0055064; P:chloride ion homeostasis; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; IMP:PomBase.
DR GO; GO:1903826; P:L-arginine transmembrane transport; IMP:PomBase.
DR GO; GO:1903401; P:L-lysine transmembrane transport; IMP:PomBase.
DR GO; GO:0055075; P:potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0034486; P:vacuolar transmembrane transport; IBA:GO_Central.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR Pfam; PF00324; AA_permease; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1050
FT /note="Uncharacterized transporter C18H10.16"
FT /id="PRO_0000310954"
FT TOPO_DOM 1..83
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..112
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 147..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..202
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..295
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..368
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..442
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 481..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..499
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..1050
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38329, ECO:0000255"
FT REGION 915..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 64
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 939
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1050 AA; 118132 MW; 5634CEE7FF682CAB CRC64;
MARLLTKSSQ VFDFLADRLS VRKSRRFWET QENLESSTPL LQEPQQSYRS NSFNELPPLS
RSVTFAENEQ PNEAVKLGTF EGCFIPTTLN VLSILLYLRF PWIIGEAGVL KTLLMLFISY
AVGIFTSLSI SAICTNGMVR GGGAYYAVSR SIGPELGGSI GLIFYVGQIL NTGMNISGFV
EPIISIFGKE SGTISQFLPE GYWWVFLYTT CVLAMCCILC CLGSAIFAKA SNALFVVIIL
STISIPISSI FVHPFKDPSL LVHFTGLKWS TLMKNLASAY TENEKGTGYE SFKSTFGVFF
PATAGLLAGA SMSGDLKAPS RSIPKGTISS QATTFLLYLL VILCVGASVT RTGLLLDMDV
MEHISLHPLF IISGILSSGA FSSFMGIFGA AKLLQAIARD DLIPGMFFFA KGSSYDDIPY
VAIGVTYLIT QISLFWDINM LSSMITMTFL LTFGFINLSC FLLRISSTPN FRPTFRYFNR
RTTLVGTILS FGVMFYVDRL NAFISFLIAG ILVVVIYFTC PPKNWGDVSQ GIIYHQLRKY
LLQTNKAREN IKFWRPQILL LINNPNRSEN VIRFCNSLKK GSLYILGHVI VSDDFQASMD
DLRKQQRLWH QFVLDRGIKA FVELTIAPDE VWGIRGLISS AGLGGIRPNI AVLTFINTNY
RRHRIYSGSS FSLENTSEES ESDSKKEFVE HDILPVKWVQ ILEDMLVGSV DVMVTNGFDR
LNWPKRKGEK QYIDMFPIHR ISGVGSEVNE STPTFATNFE TYTMVFQLSW ILHTASDWKQ
GCRLRLITLV EFENEIEAER ESMHQMLETF RIKADVVVLC LAAMNLDAYR YIVKNEHVRP
SKSSELENLL KDDSWWQEEK KRRGNTVDSL GPIRFPRRMS GYNFRSASFD KSAPPLSVPL
SFRLGPHMHS VKSFETESSF GNRSLSPKQE NRRTYSDSTI ESSLMPNVVR EDSSSDRLAP
KKKIGRDYSK EKLTFNDLSS RSQYIIMNEI VLKHTKNTSV LFTVLPAPLA DTHKSFRKSE
EYVDDLLIFM EGLPPCALIH SKSLTITTAL
