EMP24_SCHPO
ID EMP24_SCHPO Reviewed; 199 AA.
AC Q9P7I9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Endosomal protein P24B;
DE Flags: Precursor;
GN Name=emp24; ORFNames=SPCC24B10.17;
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).
CC -!- FUNCTION: Constituent of COPII-coated endoplasmic reticulum-derived
CC transport vesicles. Required for efficient transport of a subset of
CC secretory proteins to the Golgi (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Note=Recycles
CC between endoplasmic reticulum and Golgi. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family. {ECO:0000305}.
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DR EMBL; CU329672; CAB76226.1; -; Genomic_DNA.
DR PIR; T50424; T50424.
DR RefSeq; NP_588020.1; NM_001023011.2.
DR AlphaFoldDB; Q9P7I9; -.
DR SMR; Q9P7I9; -.
DR BioGRID; 275916; 10.
DR STRING; 4896.SPCC24B10.17.1; -.
DR MaxQB; Q9P7I9; -.
DR PaxDb; Q9P7I9; -.
DR PRIDE; Q9P7I9; -.
DR EnsemblFungi; SPCC24B10.17.1; SPCC24B10.17.1:pep; SPCC24B10.17.
DR GeneID; 2539350; -.
DR KEGG; spo:SPCC24B10.17; -.
DR PomBase; SPCC24B10.17; emp24.
DR VEuPathDB; FungiDB:SPCC24B10.17; -.
DR eggNOG; KOG1692; Eukaryota.
DR HOGENOM; CLU_066963_4_0_1; -.
DR InParanoid; Q9P7I9; -.
DR OMA; WNLFVIG; -.
DR PhylomeDB; Q9P7I9; -.
DR Reactome; R-SPO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:Q9P7I9; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISO:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:PomBase.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006621; P:protein retention in ER lumen; IBA:GO_Central.
DR InterPro; IPR015720; Emp24-like.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR PANTHER; PTHR22811; PTHR22811; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SMART; SM01190; EMP24_GP25L; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..199
FT /note="Endosomal protein P24B"
FT /id="PRO_0000316579"
FT TOPO_DOM 22..168
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..113
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
SQ SEQUENCE 199 AA; 23139 MW; 35DBCA4984CF4B40 CRC64;
MAFFNVFKAV LCAYFISVVF GHGITLKPHQ RECFYENLRN NDQMSVTYQT NVGGDQLVSM
SIYNPAGQIM HQEVPNSMAQ YSFTVKNPGK YMYCFYNDAL DGESKEVLFN VHGVIYISDE
DLDANNPLLG KVRQLHDTIS KVKHEQEYFV ARERIHRNTA ESTNDRVKWW SILQTVILVS
VCVFQIFYLK RLFEVKRVV
