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GET1_SCHPO
ID   GET1_SCHPO              Reviewed;         171 AA.
AC   Q9HGM2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Protein get1 {ECO:0000255|HAMAP-Rule:MF_03113};
DE   AltName: Full=Guided entry of tail-anchored proteins 1 {ECO:0000255|HAMAP-Rule:MF_03113};
GN   Name=get1; ORFNames=SPBC543.10;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, 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   -!- FUNCTION: Required for the post-translational delivery of tail-anchored
CC       (TA) proteins to the endoplasmic reticulum. Acts as a membrane receptor
CC       for soluble get3, which recognizes and selectively binds the
CC       transmembrane domain of TA proteins in the cytosol. {ECO:0000255|HAMAP-
CC       Rule:MF_03113}.
CC   -!- SUBUNIT: Interacts with get3. {ECO:0000255|HAMAP-Rule:MF_03113}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03113, ECO:0000269|PubMed:16823372}; Multi-
CC       pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03113,
CC       ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the WRB/GET1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03113}.
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DR   EMBL; CU329671; CAC05252.1; -; Genomic_DNA.
DR   RefSeq; NP_596798.1; NM_001023818.2.
DR   AlphaFoldDB; Q9HGM2; -.
DR   SMR; Q9HGM2; -.
DR   BioGRID; 277409; 61.
DR   STRING; 4896.SPBC543.10.1; -.
DR   iPTMnet; Q9HGM2; -.
DR   MaxQB; Q9HGM2; -.
DR   PaxDb; Q9HGM2; -.
DR   PRIDE; Q9HGM2; -.
DR   EnsemblFungi; SPBC543.10.1; SPBC543.10.1:pep; SPBC543.10.
DR   GeneID; 2540893; -.
DR   KEGG; spo:SPBC543.10; -.
DR   PomBase; SPBC543.10; get1.
DR   VEuPathDB; FungiDB:SPBC543.10; -.
DR   eggNOG; KOG4253; Eukaryota.
DR   HOGENOM; CLU_089418_1_0_1; -.
DR   InParanoid; Q9HGM2; -.
DR   OMA; WFGPLTW; -.
DR   PhylomeDB; Q9HGM2; -.
DR   PRO; PR:Q9HGM2; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043529; C:GET complex; ISO:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032977; F:membrane insertase activity; IC:PomBase.
DR   GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IC:PomBase.
DR   Gene3D; 1.10.287.660; -; 1.
DR   HAMAP; MF_03113; Get1; 1.
DR   InterPro; IPR028945; Get1.
DR   InterPro; IPR027538; Get1_fungi.
DR   InterPro; IPR029012; Helix_hairpin_bin_sf.
DR   Pfam; PF04420; CHD5; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..171
FT                   /note="Protein get1"
FT                   /id="PRO_0000372625"
FT   TOPO_DOM        1..4
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        5..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        25..108
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        130..153
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TRANSMEM        154..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   TOPO_DOM        171
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   COILED          38..95
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   171 AA;  20192 MW;  7A251A5F5E5F9FBF CRC64;
     MMDLIISTIL LSLFIHFFDK FAKKRTIDGA YRIYVSVSNN KDLKKNKEIL EQLLTVKKEL
     NATSSQDQFA KWARLNRKYE QLSQEWEKQS ANVKIFQDTF KRVLSLFLWI LTRGFRFYIQ
     FKESKTPVFF LPAFLLPSWA LWVLSLPRSI YGSVSLTVWN FAVQKTISGI F
 
 
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