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SLPI_SCHPO
ID   SLPI_SCHPO              Reviewed;         659 AA.
AC   O59729;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Uncharacterized protein slp1 {ECO:0000250|UniProtKB:Q12232};
DE   AltName: Full=SUN-like protein 1 {ECO:0000250|UniProtKB:Q12232};
DE   Flags: Precursor;
GN   ORFNames=SPBC3E7.09 {ECO:0000312|PomBase:SPBC3E7.09};
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).
CC   -!- FUNCTION: May be involved in membrane protein folding.
CC       {ECO:0000250|UniProtKB:Q12232}.
CC   -!- SUBUNIT: Interacts with EMP65. {ECO:0000250|UniProtKB:Q12232}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q12232}; Single-pass type I membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the SLP1 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA19012.1; -; Genomic_DNA.
DR   PIR; T40383; T40383.
DR   RefSeq; NP_596096.1; NM_001022012.2.
DR   AlphaFoldDB; O59729; -.
DR   SMR; O59729; -.
DR   BioGRID; 276806; 1.
DR   STRING; 4896.SPBC3E7.09.1; -.
DR   iPTMnet; O59729; -.
DR   MaxQB; O59729; -.
DR   PaxDb; O59729; -.
DR   PRIDE; O59729; -.
DR   EnsemblFungi; SPBC3E7.09.1; SPBC3E7.09.1:pep; SPBC3E7.09.
DR   GeneID; 2540275; -.
DR   KEGG; spo:SPBC3E7.09; -.
DR   PomBase; SPBC3E7.09; -.
DR   VEuPathDB; FungiDB:SPBC3E7.09; -.
DR   eggNOG; KOG1396; Eukaryota.
DR   HOGENOM; CLU_416284_0_0_1; -.
DR   InParanoid; O59729; -.
DR   OMA; YESSWME; -.
DR   PhylomeDB; O59729; -.
DR   PRO; PR:O59729; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; ISO:PomBase.
DR   InterPro; IPR045120; Suco/Slp1-like.
DR   InterPro; IPR012919; SUN_dom.
DR   PANTHER; PTHR12953; PTHR12953; 1.
DR   Pfam; PF07738; Sad1_UNC; 1.
DR   PROSITE; PS51469; SUN; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..659
FT                   /note="Uncharacterized protein slp1"
FT                   /id="PRO_0000363387"
FT   TOPO_DOM        26..556
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q12232"
FT   TRANSMEM        557..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        575..659
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q12232"
FT   DOMAIN          173..335
FT                   /note="SUN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00802"
FT   REGION          417..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          632..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        393
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        415
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        504
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   659 AA;  74072 MW;  B0AC716FA05263CC CRC64;
     MVKRRLSAFG NAFLIYFIIF RLCCCSPQTS HWCKYPALCL KSPDTHNENL VCDAYLSVIA
     TKSEEKEASN PTTWDFTPTN KYQEPSFHTK TSLNGSDTIS SNFLSKYEYS NGTSTSEFID
     SISPPLVNET STISSSKKLE QNYSVTEVID TNIITSSSVT LPISEDGSST SAAATIDSNI
     DEKTVAFSEE KRFNFASTDC AAAVIKTNPE AVGSSSILTE NKDKYMLNKC SAENKFVVIE
     LCEDIYVDTV QIANFEFFSS IFRDFKVSVS GKYPKYESSW MELGTFTALN LRTLQSFHIE
     NPLIWAKYLK IEFLTHYGSE FYCPVSLLRV YGKTMIEEFE EANEDFLEQK VNDGSAIKAD
     EIRKPQESPI FVDEEDTDVQ SKPVRKNPSV ELNSTDTLLS STVISKSLST VVIGNETGKS
     ESYPATSTRS FNDISPSSSS SYSTAQISTF PSNQESIYKN INKRLSTLEE RKKAFDEIVE
     KILTNYGKHN AKNMNFTQLL HELNSTLQLE ISKLSKSVVK PSLFALQAKL ELLSAENEYF
     QSQITSLYQE SSFQKRLLML QLTVLIVLTV YMAVSRLPEN LPTTRSSSNN PIEASRPPFS
     RDEQDISKAN DFRVSASSAV YTVGPELLQR KKRDPNTSIR SIHEREQDKI IHSRSHSVC
 
 
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