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SPCS2_DROME
ID   SPCS2_DROME             Reviewed;         199 AA.
AC   Q9VYY2;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Signal peptidase complex subunit 2;
DE   AltName: Full=Microsomal signal peptidase 25 kDa subunit;
DE            Short=SPase 25 kDa subunit;
GN   Name=Spase25; ORFNames=CG1751;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=15901661; DOI=10.1242/dev.01863;
RA   Abrams E.W., Andrew D.J.;
RT   "CrebA regulates secretory activity in the Drosophila salivary gland and
RT   epidermis.";
RL   Development 132:2743-2758(2005).
CC   -!- FUNCTION: Component of the signal peptidase complex (SPC) which
CC       catalyzes the cleavage of N-terminal signal sequences from nascent
CC       proteins as they are translocated into the lumen of the endoplasmic
CC       reticulum (By similarity). Enhances the enzymatic activity of SPC and
CC       facilitates the interactions between different components of the
CC       translocation site (By similarity). {ECO:0000250|UniProtKB:Q04969,
CC       ECO:0000250|UniProtKB:Q15005}.
CC   -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC       catalytic subunit twr/SEC11 and three accessory subunits Spase12/SPCS1,
CC       Spase25/SPCS2 and Spase22-23/SPCS3. The complex induces a local
CC       thinning of the ER membrane which is used to measure the length of the
CC       signal peptide (SP) h-region of protein substrates. This ensures the
CC       selectivity of the complex towards h-regions shorter than 18-20 amino
CC       acids. {ECO:0000250|UniProtKB:Q15005}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q28250}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q28250}.
CC   -!- SIMILARITY: Belongs to the SPCS2 family. {ECO:0000305}.
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DR   EMBL; AE014298; AAF48051.1; -; Genomic_DNA.
DR   EMBL; AY094832; AAM11185.1; -; mRNA.
DR   RefSeq; NP_001285124.1; NM_001298195.1.
DR   RefSeq; NP_001285125.1; NM_001298196.1.
DR   RefSeq; NP_572723.1; NM_132495.3.
DR   AlphaFoldDB; Q9VYY2; -.
DR   SMR; Q9VYY2; -.
DR   IntAct; Q9VYY2; 22.
DR   STRING; 7227.FBpp0073355; -.
DR   PaxDb; Q9VYY2; -.
DR   PRIDE; Q9VYY2; -.
DR   DNASU; 32095; -.
DR   EnsemblMetazoa; FBtr0073506; FBpp0073355; FBgn0030306.
DR   EnsemblMetazoa; FBtr0340293; FBpp0309254; FBgn0030306.
DR   EnsemblMetazoa; FBtr0340294; FBpp0309255; FBgn0030306.
DR   GeneID; 32095; -.
DR   KEGG; dme:Dmel_CG1751; -.
DR   CTD; 32095; -.
DR   FlyBase; FBgn0030306; Spase25.
DR   VEuPathDB; VectorBase:FBgn0030306; -.
DR   eggNOG; KOG4072; Eukaryota.
DR   GeneTree; ENSGT00440000038181; -.
DR   HOGENOM; CLU_094622_0_0_1; -.
DR   InParanoid; Q9VYY2; -.
DR   OMA; DMRKYDD; -.
DR   OrthoDB; 1395649at2759; -.
DR   PhylomeDB; Q9VYY2; -.
DR   BioGRID-ORCS; 32095; 1 hit in 1 CRISPR screen.
DR   ChiTaRS; Spase25; fly.
DR   GenomeRNAi; 32095; -.
DR   PRO; PR:Q9VYY2; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0030306; Expressed in spermathecum and 34 other tissues.
DR   ExpressionAtlas; Q9VYY2; baseline and differential.
DR   Genevisible; Q9VYY2; DM.
DR   GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central.
DR   GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR   GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR   InterPro; IPR009582; Spc2/SPCS2.
DR   PANTHER; PTHR13085; PTHR13085; 1.
DR   Pfam; PF06703; SPC25; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..199
FT                   /note="Signal peptidase complex subunit 2"
FT                   /id="PRO_0000221166"
FT   TOPO_DOM        1..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
FT   TRANSMEM        50..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        73..81
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
FT   TRANSMEM        82..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        105..199
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q28250"
SQ   SEQUENCE   199 AA;  22216 MW;  81E8D652851E7643 CRC64;
     MGKKDEKSQQ GEELVKVNKW DGSAVKHALD DAVKTCLLGD RPQLKEQFGL VNTRLALCAL
     AVSVAIMAHA WDFTHPFPES RPVLLFSVLA YFALLGILTL HSSFREKGTF AVALQKDKER
     ERLWEASSDM RKYDDKYLLT LSVRDTKNGK RREQSSNKSC AAFIDQNGIV LDNLVANEVN
     RLFNALAADK KNASSLSSN
 
 
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