MUG69_SCHPO
ID MUG69_SCHPO Reviewed; 192 AA.
AC O14193;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 4.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=SRP-independent targeting protein 2 homolog {ECO:0000250|UniProtKB:Q99382};
DE AltName: Full=Meiotically up-regulated gene 69 protein {ECO:0000303|PubMed:16303567};
GN Name=mug69 {ECO:0000303|PubMed:16303567};
GN ORFNames=SPAC56E4.05 {ECO:0000312|PomBase:SPAC56E4.05};
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
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).
CC -!- FUNCTION: May function in a SRP (signal recognition particle) and GET
CC (guided entry of tail-anchored proteins) independent pathway for
CC targeting a broad range of substrate proteins to the endoplasmic
CC reticulum (By similarity). Has a role in meiosis (PubMed:16303567).
CC {ECO:0000250|UniProtKB:Q99382, ECO:0000269|PubMed:16303567}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the TMEM208 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16396.2; -; Genomic_DNA.
DR PIR; T38907; T38907.
DR RefSeq; NP_593272.1; NM_001018669.2.
DR AlphaFoldDB; O14193; -.
DR BioGRID; 279646; 4.
DR STRING; 4896.SPAC56E4.05.1; -.
DR MaxQB; O14193; -.
DR PaxDb; O14193; -.
DR EnsemblFungi; SPAC56E4.05.1; SPAC56E4.05.1:pep; SPAC56E4.05.
DR GeneID; 2543218; -.
DR KEGG; spo:SPAC56E4.05; -.
DR PomBase; SPAC56E4.05; mug69.
DR VEuPathDB; FungiDB:SPAC56E4.05; -.
DR eggNOG; KOG3269; Eukaryota.
DR HOGENOM; CLU_094308_2_1_1; -.
DR InParanoid; O14193; -.
DR OMA; LYWTWGC; -.
DR PhylomeDB; O14193; -.
DR PRO; PR:O14193; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045048; P:protein insertion into ER membrane; ISO:PomBase.
DR GO; GO:0045047; P:protein targeting to ER; ISO:PomBase.
DR GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central.
DR InterPro; IPR008506; SND2/TMEM208.
DR PANTHER; PTHR13505; PTHR13505; 1.
DR Pfam; PF05620; TMEM208_SND2; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Meiosis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..192
FT /note="SRP-independent targeting protein 2 homolog"
FT /id="PRO_0000278503"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 149..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 192 AA; 22104 MW; C36C7F3B04D7145E CRC64;
MANAAQKKLA AQNKHILTFM LAADLIVNVL FWILRFFVRS GLSKFSKFVY AFASISSGFL
HYQLHRAAAP KYDARGSLLY VGQDLLQEGV TSYMVDYMYF SWILIFLAAL TSVKVFAFYL
LVPIFVVYKA APLLKMLLQQ LKNFKNQALN QPPQQQQQQQ QQQHQQHATP SEPVLSKRQQ
KLRKKAAKYS RP
