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SPCS1_ARATH
ID   SPCS1_ARATH             Reviewed;          92 AA.
AC   Q944J0; Q7G9Y5;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Signal peptidase complex subunit 1;
DE   AltName: Full=Microsomal signal peptidase 12 kDa subunit;
DE            Short=SPase 12 kDa subunit;
GN   OrderedLocusNames=At2g22425; ORFNames=F14M13.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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). Dispensable for SPC enzymatic activity (By
CC       similarity). {ECO:0000250|UniProtKB:P46965,
CC       ECO:0000250|UniProtKB:Q9Y6A9}.
CC   -!- SUBUNIT: Component of the signal peptidase complex (SPC) composed of a
CC       catalytic subunit SEC11 and three accessory subunits SPCS1, SPCS2 and
CC       SPCS3. The complex induces a local thinning of the ER membrane which is
CC       used to measure the length of the signal peptide (SP) h-region of
CC       protein substrates. This ensures the selectivity of the complex towards
CC       h-regions shorter than 18-20 amino acids.
CC       {ECO:0000250|UniProtKB:Q9Y6A9}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P83362}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P83362}.
CC   -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
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DR   EMBL; AC006592; AAM15302.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07302.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07303.1; -; Genomic_DNA.
DR   EMBL; AF428383; AAL16151.1; -; mRNA.
DR   EMBL; AY143801; AAN28740.1; -; mRNA.
DR   EMBL; AY087762; AAM65298.1; -; mRNA.
DR   RefSeq; NP_001077942.1; NM_001084473.2.
DR   RefSeq; NP_565535.1; NM_127807.4.
DR   AlphaFoldDB; Q944J0; -.
DR   SMR; Q944J0; -.
DR   BioGRID; 2127; 172.
DR   IntAct; Q944J0; 172.
DR   STRING; 3702.AT2G22425.1; -.
DR   PaxDb; Q944J0; -.
DR   PRIDE; Q944J0; -.
DR   ProteomicsDB; 232632; -.
DR   EnsemblPlants; AT2G22425.1; AT2G22425.1; AT2G22425.
DR   EnsemblPlants; AT2G22425.2; AT2G22425.2; AT2G22425.
DR   GeneID; 816774; -.
DR   Gramene; AT2G22425.1; AT2G22425.1; AT2G22425.
DR   Gramene; AT2G22425.2; AT2G22425.2; AT2G22425.
DR   KEGG; ath:AT2G22425; -.
DR   Araport; AT2G22425; -.
DR   TAIR; locus:505006266; AT2G22425.
DR   eggNOG; KOG4112; Eukaryota.
DR   HOGENOM; CLU_134505_0_1_1; -.
DR   InParanoid; Q944J0; -.
DR   OMA; FRAMMLI; -.
DR   PhylomeDB; Q944J0; -.
DR   PRO; PR:Q944J0; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q944J0; baseline and differential.
DR   Genevisible; Q944J0; AT.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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; IPR009542; Spc1/SPCS1.
DR   PANTHER; PTHR13202; PTHR13202; 1.
DR   Pfam; PF06645; SPC12; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..92
FT                   /note="Signal peptidase complex subunit 1"
FT                   /id="PRO_0000215160"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        13..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..36
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   TRANSMEM        37..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P83362"
FT   REGION          73..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   92 AA;  10373 MW;  E626DBFBA6D03587 CRC64;
     MDWQGQKLVE QLMQILLVIS GVVAVVVGYT TESFRTMMLI YAGGVVLTTL VTVPNWPFYN
     LHPLKWLDPS EAEKHPKPEV VSVASKKKFS KK
 
 
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