ERD11_SCHPO
ID ERD11_SCHPO Reviewed; 373 AA.
AC Q9UTD8; Q9C0Z2;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Protein ERD1 homolog 1;
GN Name=erd1; ORFNames=SPAC227.01c, SPAPB21F2.04c;
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).
CC -!- FUNCTION: Required for the retention of luminal endoplasmic reticulum
CC proteins, affects glycoprotein processing in the Golgi apparatus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16823372};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Endoplasmic
CC reticulum membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ERD1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAC36893.1; -; Genomic_DNA.
DR PIR; T50157; T50157.
DR RefSeq; NP_592955.2; NM_001018355.2.
DR AlphaFoldDB; Q9UTD8; -.
DR BioGRID; 278399; 70.
DR STRING; 4896.SPAC227.01c.1; -.
DR MaxQB; Q9UTD8; -.
DR PaxDb; Q9UTD8; -.
DR EnsemblFungi; SPAC227.01c.1; SPAC227.01c.1:pep; SPAC227.01c.
DR GeneID; 2541909; -.
DR KEGG; spo:SPAC227.01c; -.
DR PomBase; SPAC227.01c; erd1.
DR VEuPathDB; FungiDB:SPAC227.01c; -.
DR eggNOG; KOG1162; Eukaryota.
DR HOGENOM; CLU_024081_2_1_1; -.
DR InParanoid; Q9UTD8; -.
DR OMA; WIFLRVE; -.
DR PhylomeDB; Q9UTD8; -.
DR PRO; PR:Q9UTD8; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:PomBase.
DR GO; GO:0006621; P:protein retention in ER lumen; IMP:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR004342; EXS_C.
DR Pfam; PF03124; EXS; 1.
DR PROSITE; PS51380; EXS; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..373
FT /note="Protein ERD1 homolog 1"
FT /id="PRO_0000116788"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 178..373
FT /note="EXS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00712"
SQ SEQUENCE 373 AA; 43627 MW; 33BFED69BFFB0FAF CRC64;
MALIEDLNHF INYFPLVLRL FFLVVFGLYS FTLILHLLVI NRVDVFSLLH TPLPVNRSQQ
ANAPLWQLSF SLSILGTLLF VIAESLYLIS GSDELAYVPV FIFGVIVFMP VHKFWFFQRK
VFTRQCLRIL GGSYRPDYKF PDVIFSDLLT SYSRVIADLW LAGAILIYVT DSPNNSHRKQ
YENEVIMSMI AAYPYAIRFR QCLIERSSAD NSSDKFWSTL NSIKYFTAFP AIFLGIFAKK
RFSFLWFLWN TSSAINSTYS FWWDVSMDWS LPFFKQPLSI QNWKFGVRRL FPTFTFAVVS
AIDFVLRMAW VVRVLPEHQS AFFTTDFGIF IMQFLEVFRR CVWVFFRIEA EASKSLAYVN
ISDRSDIPTI HPD
