CIS4_SCHPO
ID CIS4_SCHPO Reviewed; 732 AA.
AC Q9HGQ3; P78888;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable zinc transporter cis4;
GN Name=cis4; ORFNames=SPAC17D4.03c;
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 MRNA] OF 377-732.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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 FUNCTION, MUTAGENESIS OF GLY-375 AND GLY-393, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH ZRG17.
RX PubMed=18199682; DOI=10.1091/mbc.e07-08-0805;
RA Fang Y., Sugiura R., Ma Y., Yada-Matsushima T., Umeno H., Kuno T.;
RT "Cation diffusion facilitator Cis4 is implicated in Golgi membrane
RT trafficking via regulating zinc homeostasis in fission yeast.";
RL Mol. Biol. Cell 19:1295-1303(2008).
CC -!- FUNCTION: Probable zinc transporter involved in Golgi membrane
CC trafficking through the regulation of zinc homeostasis.
CC {ECO:0000269|PubMed:18199682}.
CC -!- SUBUNIT: Interacts with zrg17. {ECO:0000269|PubMed:18199682}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein. Golgi apparatus, cis-Golgi network membrane; Multi-
CC pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC transporter (TC 2.A.4) family. SLC30A subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAC05733.1; -; Genomic_DNA.
DR EMBL; D89239; BAA13900.1; -; mRNA.
DR PIR; T43145; T43145.
DR RefSeq; NP_594694.1; NM_001020122.2.
DR AlphaFoldDB; Q9HGQ3; -.
DR BioGRID; 278720; 45.
DR IntAct; Q9HGQ3; 1.
DR STRING; 4896.SPAC17D4.03c.1; -.
DR MaxQB; Q9HGQ3; -.
DR PaxDb; Q9HGQ3; -.
DR EnsemblFungi; SPAC17D4.03c.1; SPAC17D4.03c.1:pep; SPAC17D4.03c.
DR GeneID; 2542250; -.
DR KEGG; spo:SPAC17D4.03c; -.
DR PomBase; SPAC17D4.03c; cis4.
DR VEuPathDB; FungiDB:SPAC17D4.03c; -.
DR eggNOG; KOG1484; Eukaryota.
DR HOGENOM; CLU_385941_0_0_1; -.
DR InParanoid; Q9HGQ3; -.
DR OMA; HMAFDCI; -.
DR PhylomeDB; Q9HGQ3; -.
DR Reactome; R-SPO-264876; Insulin processing.
DR Reactome; R-SPO-435368; Zinc efflux and compartmentalization by the SLC30 family.
DR PRO; PR:Q9HGQ3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IMP:PomBase.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:PomBase.
DR GO; GO:0030001; P:metal ion transport; IBA:GO_Central.
DR GO; GO:1904257; P:zinc ion import into Golgi apparatus; IMP:PomBase.
DR GO; GO:0062111; P:zinc ion import into organelle; IDA:PomBase.
DR Gene3D; 1.20.1510.10; -; 2.
DR InterPro; IPR002524; Cation_efflux.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR InterPro; IPR045316; Msc2-like.
DR PANTHER; PTHR45755; PTHR45755; 1.
DR Pfam; PF01545; Cation_efflux; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
DR TIGRFAMs; TIGR01297; CDF; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..732
FT /note="Probable zinc transporter cis4"
FT /id="PRO_0000206116"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 526..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 375
FT /note="G->E: In cis4-1; confers sensitivities to the
FT calcineurin inhibitor FK506 and to a high concentration of
FT MgCl2."
FT /evidence="ECO:0000269|PubMed:18199682"
FT MUTAGEN 393
FT /note="G->D: In cis4-2; confers sensitivities to the
FT calcineurin inhibitor FK506 and to a high concentration of
FT MgCl2."
FT /evidence="ECO:0000269|PubMed:18199682"
FT CONFLICT 618
FT /note="L -> S (in Ref. 2; BAA13900)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="N -> H (in Ref. 2; BAA13900)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="I -> V (in Ref. 2; BAA13900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 82740 MW; DBA5452D4329CB0B CRC64;
MNVNSSAFER TNRFPSFPVL KDDQKTSSDS IAAAKKKDLL SLISSKSLLS SETLGWFSVI
CAFSITGSGL EVNTMSIPFY LIFGIFAFVS FTTQYLGIYS FSFQPFQLLN VIIASLSMVF
ITLGAFVLGT LDTTCLLLLA FKLFFIRNDP TPFNARSANL KNYIAFPICL FVINHILILL
GYFQCSYSVF YASVFYILLG VFIRVFYLVN KEKFEKKELA FLFSSIVVAC LIQFNVLPLG
TINLSVTRFT ILCFMQIFCI NWDGIARIQF YLGKFDISLI MALISAIINK TASQNSIKII
SCLYQVGFCF FKIGSSITAN LKLPDNSRIY RLYNDFIVNG VLADKESRSI FYFFLLNVSY
MFVQVIYGLW TNSLGLISDA IHMAFDCIAI LVGLVATTLA KMPLNYAYPF GFAKIEALSG
FTNGIFLVLI SFSIVGEALY RLFHPPQMNT DQLLLVSFLG LVVNLVGILA FNHGHNHDHG
SHHHHSHSNH SMCLPNTTND INIFEEFEEE KDNVEAQKMG YTNDDHVSQH EHTHENSQEH
HHEHNHNHDH IHKYNEKCDH ESISLQNLDN DHHCHHHHEN HNMHGIFLHI IADTMGSVGV
IVSTILIQWF SWTGFDPLAS LIIAALIFVS VLPLIKDSAK NLLSVTDPES EYLLKQCLSN
ISLSNSVISL SNPKFWTNER GEVYGILHIQ VSIDGDLNVV RNEVFRKLSI AVPNLKHICI
QSERPNNCWC GK
