ID SHR3_SCHPO Reviewed; 215 AA.
AC Q9Y876;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 10-JUN-2026, entry version 138.
DE RecName: Full=Secretory component protein psh3;
GN Name=psh3; ORFNames=SPBC409.20c;
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 [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11069779; DOI=10.1242/jcs.113.23.4351;
RA Martinez P., Ljungdahl P.O.;
RT "The SHR3 homologue from S. pombe demonstrates a conserved function of ER
RT packaging chaperones.";
RL J. Cell Sci. 113:4351-4362(2000).
RN [2]
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).
CC -!- FUNCTION: Involved in amino acid permease processing and required for
CC the efficient translocation of structurally related amino acid
CC permeases from the endoplasmic reticulum to the plasma membrane.
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11069779}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11069779}.
CC -!- SIMILARITY: To yeast SHR3. {ECO:0000305}.
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DR EMBL; AF160498; AAD44978.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB52622.1; -; Genomic_DNA.
DR PIR; T40447; T40447.
DR RefSeq; NP_595470.1; NM_001021380.2.
DR AlphaFoldDB; Q9Y876; -.
DR BioGRID; 277319; 102.
DR FunCoup; Q9Y876; 95.
DR STRING; 284812.Q9Y876; -.
DR iPTMnet; Q9Y876; -.
DR PaxDb; 284812-Q9Y876; -.
DR GeneID; 2540800; -.
DR KEGG; spo:2540800; -.
DR PomBase; SPBC409.20c; psh3.
DR VEuPathDB; FungiDB:SPBC409.20c; -.
DR eggNOG; ENOG502T3NF; Eukaryota.
DR HOGENOM; CLU_1283927_0_0_1; -.
DR InParanoid; Q9Y876; -.
DR OMA; DAYYSFL; -.
DR PhylomeDB; Q9Y876; -.
DR PRO; PR:Q9Y876; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0044183; F:protein folding chaperone; ISO:PomBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0045048; P:protein insertion into ER membrane; ISO:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR013248; Psh3/Shr3.
DR PANTHER; PTHR28228; SECRETORY COMPONENT PROTEIN SHR3; 1.
DR PANTHER; PTHR28228:SF1; SECRETORY COMPONENT PROTEIN SHR3; 1.
DR Pfam; PF08229; SHR3_chaperone; 1.
DR PIRSF; PIRSF029187; Shr3_AAP_chap; 1.
DR SMART; SM00786; SHR3_chaperone; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..215
FT /note="Secretory component protein psh3"
FT /id="PRO_0000097739"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 190..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..215
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 215 AA; 24060 MW; 1663059E467AEA28 CRC64;
MAKRSIFRFA DEKGLKVAAR YGVLMSTSFI FALLFHSSVA DVNTLWSPGP ESAFDAAETY
YTLVAGSHFI VKYTVYTIMG LNMIFHLIQA TGAKGDDKLF FYSSTLLYLT ALILFIVNVA
PSMLVVKLQN YVQFPRNMHL SVLAASHVLV EFLLAGVILI QLGYVFGYHV QSIQQREYAE
DMREQELAEK AKLESESATT QSVETVSTES VSKRK
//
