ID   TTS1_SCHPO              Reviewed;         279 AA.
AC   Q9Y7Z5;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Tetra-spanning protein 1;
GN   Name=tts1; ORFNames=SPBC1539.04;
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   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   [3]
RP   SUBCELLULAR LOCATION, INTERACTION WITH RTN1 AND YOP1, AND FUNCTION.
RX   PubMed=20434336; DOI=10.1016/j.cub.2010.04.017;
RA   Zhang D., Vjestica A., Oliferenko S.;
RT   "The cortical ER network limits the permissive zone for actomyosin ring
RT   assembly.";
RL   Curr. Biol. 20:1029-1034(2010).
CC   -!- FUNCTION: Required for the correct positioning of the cellular division
CC       plane by delimiting the actomyosin ring assembly at the cell equator.
CC       {ECO:0000269|PubMed:20434336}.
CC   -!- SUBUNIT: Interacts with RTN1 and YOP1. {ECO:0000269|PubMed:20434336}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane
CC       protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC       Nucleus membrane; Multi-pass membrane protein. Note=Enriched at the
CC       cell equator during mitosis.
CC   -!- SIMILARITY: Belongs to the PER33/POM33 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAB51336.1; -; Genomic_DNA.
DR   PIR; T39463; T39463.
DR   RefSeq; NP_596818.1; NM_001023838.2.
DR   AlphaFoldDB; Q9Y7Z5; -.
DR   BioGRID; 276467; 7.
DR   STRING; 4896.SPBC1539.04.1; -.
DR   TCDB; 8.A.124.1.1; the tetra spanning protein 1 (tts1) family.
DR   iPTMnet; Q9Y7Z5; -.
DR   MaxQB; Q9Y7Z5; -.
DR   PaxDb; Q9Y7Z5; -.
DR   PRIDE; Q9Y7Z5; -.
DR   EnsemblFungi; SPBC1539.04.1; SPBC1539.04.1:pep; SPBC1539.04.
DR   GeneID; 2539923; -.
DR   KEGG; spo:SPBC1539.04; -.
DR   PomBase; SPBC1539.04; tts1.
DR   VEuPathDB; FungiDB:SPBC1539.04; -.
DR   eggNOG; KOG4002; Eukaryota.
DR   HOGENOM; CLU_065417_0_0_1; -.
DR   InParanoid; Q9Y7Z5; -.
DR   OMA; VSYAIVC; -.
DR   PhylomeDB; Q9Y7Z5; -.
DR   PRO; PR:Q9Y7Z5; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0032153; C:cell division site; IDA:PomBase.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR   GO; GO:0031965; C:nuclear membrane; IDA:PomBase.
DR   GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:1990809; P:endoplasmic reticulum tubular network membrane organization; IMP:PomBase.
DR   GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IBA:GO_Central.
DR   GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR   GO; GO:0140480; P:mitotic spindle pole body insertion into the nuclear envelope; IGI:PomBase.
DR   GO; GO:1990608; P:mitotic spindle pole body localization; IGI:PomBase.
DR   GO; GO:0071763; P:nuclear membrane organization; IMP:PomBase.
DR   InterPro; IPR005344; TMEM33/Pom33.
DR   Pfam; PF03661; TMEM33_Pom33; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Endoplasmic reticulum; Glycoprotein;
KW   Golgi apparatus; Membrane; Nucleus; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..279
FT                   /note="Tetra-spanning protein 1"
FT                   /id="PRO_0000351445"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          260..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   279 AA;  31570 MW;  FC5FADA9555E7017 CRC64;
     MEPKQRVVKP LKERVLPVVK NTQFVWFSGQ VIVLISSVLY ALQAIPFRSA PPFLFKSAAF
     GAIVAYAIVL YKTYSPNLTS RASWNKHFFA RLMLDDNVQY FILALSMLID RPILFSLAPY
     AIYATFHIST YLRSVLLPAI YPNISDAKTA SYASRVSNLL NQYTRSQFQP AMQLVASLET
     FLLFRLFFGV FLRKNSISRL VGYIFFLRMR YTNSHFTRAS IKAVSLRMDR LVADNRVPPV
     IKNAWHTFKT YVSKFGASPV GTAQSRPTAS SSTTAPSST