ERV41_SCHPO
ID ERV41_SCHPO Reviewed; 333 AA.
AC O94283;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=ER-derived vesicles protein 41;
GN Name=erv41; ORFNames=SPBC2G5.04c;
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-317 AND SER-319, AND
RP IDENTIFICATION BY 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: Constituent of COPII-coated endoplasmic reticulum-derived
CC transport vesicles. Required for efficient transport of a subset of
CC secretory proteins to the Golgi. Facilitates retrograde transport from
CC the Golgi to the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}. Endoplasmic reticulum-Golgi intermediate
CC compartment membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:16823372}. Note=Recycles between
CC endoplasmic reticulum and Golgi. Resides in the endoplasmic and Golgi
CC compartments, and then packaged into endoplasmic reticulum derived
CC vesicles (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ERGIC family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21880.1; -; Genomic_DNA.
DR PIR; T40161; T40161.
DR RefSeq; NP_596065.1; NM_001021976.2.
DR AlphaFoldDB; O94283; -.
DR SMR; O94283; -.
DR BioGRID; 276841; 2.
DR STRING; 4896.SPBC2G5.04c.1; -.
DR iPTMnet; O94283; -.
DR SwissPalm; O94283; -.
DR MaxQB; O94283; -.
DR PaxDb; O94283; -.
DR PRIDE; O94283; -.
DR EnsemblFungi; SPBC2G5.04c.1; SPBC2G5.04c.1:pep; SPBC2G5.04c.
DR GeneID; 2540311; -.
DR KEGG; spo:SPBC2G5.04c; -.
DR PomBase; SPBC2G5.04c; erv41.
DR VEuPathDB; FungiDB:SPBC2G5.04c; -.
DR eggNOG; KOG2667; Eukaryota.
DR HOGENOM; CLU_034705_2_0_1; -.
DR InParanoid; O94283; -.
DR OMA; TYQYSVK; -.
DR PhylomeDB; O94283; -.
DR PRO; PR:O94283; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISO:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISO:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR InterPro; IPR045888; Erv.
DR InterPro; IPR012936; Erv_C.
DR InterPro; IPR039542; Erv_N.
DR PANTHER; PTHR10984; PTHR10984; 1.
DR Pfam; PF07970; COPIIcoated_ERV; 1.
DR Pfam; PF13850; ERGIC_N; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; ER-Golgi transport; Glycoprotein; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..333
FT /note="ER-derived vesicles protein 41"
FT /id="PRO_0000337254"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..285
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 333 AA; 37610 MW; D1BB509EF3D4D57F CRC64;
MLRSRVPANI RAFDAFPKFS KEYRRQSSSR GGFFTILLSV LIVVLVFSQC VQYIRGIREQ
ELFIYDSVSE LMDLNIDITI AMPCSNLRID VVDRTKDLVL ATEALTLEEA FIKDMPTSST
IYKNDRYAGL RWARTEKFRK KNNAEPGSGT ACRIYGQLVV NRVNGQLHIT APGWGYGRSN
IPFHSLNFTH YIEELSFGEY YPALVNALDG HYGHANDHPF AFQYYLSVLP TSYKSSFRSF
ETNQYSLTEN SVVRQLGFGS LPPGIFIDYD LEPLAVRVVD KHPNVASTLL RILAISGGLI
TVASWIERVY SSRAHRSTSE ADMLGLLGKS ETE
