SPCS1_CANLF
ID SPCS1_CANLF Reviewed; 102 AA.
AC P83362; F6V6C9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Signal peptidase complex subunit 1;
DE AltName: Full=Microsomal signal peptidase 12 kDa subunit;
DE Short=SPase 12 kDa subunit;
GN Name=SPCS1; Synonyms=SPC12;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000312|Proteomes:UP000002254};
RN [1] {ECO:0000312|Proteomes:UP000002254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer {ECO:0000312|Proteomes:UP000002254};
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP PROTEIN SEQUENCE OF 1-20 AND 139-157, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND TOPOLOGY.
RC TISSUE=Pancreas {ECO:0000269|PubMed:8632014};
RX PubMed=8632014; DOI=10.1074/jbc.271.7.3925;
RA Kalies K.-U., Hartmann E.;
RT "Membrane topology of the 12- and the 25-kDa subunits of the mammalian
RT signal peptidase complex.";
RL J. Biol. Chem. 271:3925-3929(1996).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=3511473; DOI=10.1073/pnas.83.3.581;
RA Evans E.A., Gilmore R., Blobel G.;
RT "Purification of microsomal signal peptidase as a complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:581-585(1986).
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 (PubMed:3511473). Dispensable for SPC enzymatic activity (By
CC similarity). {ECO:0000250|UniProtKB:P46965,
CC ECO:0000269|PubMed:3511473}.
CC -!- SUBUNIT: Component of the signal peptidase complex paralog A (SPC-A)
CC composed of a catalytic subunit SEC11A and three accessory subunits
CC SPCS1, SPCS2 and SPCS3 (PubMed:3511473). Component of the signal
CC peptidase complex paralog C (SPC-C) composed of a catalytic subunit
CC SEC11C and three accessory subunits SPCS1, SPCS2 and SPCS3
CC (PubMed:3511473). Within the complex, interacts with SPCS2 and SPCS3
CC (By similarity). The complex induces a local thinning of the ER
CC membrane which is used to measure the length of the signal peptide (SP)
CC h-region of protein substrates (By similarity). This ensures the
CC selectivity of the complex towards h-regions shorter than 18-20 amino
CC acids (By similarity). {ECO:0000250|UniProtKB:Q9Y6A9,
CC ECO:0000269|PubMed:3511473}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8632014}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:8632014}.
CC -!- TISSUE SPECIFICITY: Expressed in the pancreas (at protein level).
CC {ECO:0000269|PubMed:3511473, ECO:0000269|PubMed:8632014}.
CC -!- PTM: May be phosphorylated. {ECO:0000250|UniProtKB:Q9Y6A9}.
CC -!- SIMILARITY: Belongs to the SPCS1 family. {ECO:0000305}.
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DR EMBL; AAEX03012192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX03012193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX03012194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX03012195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX03012196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_533796.3; XM_533796.5.
DR AlphaFoldDB; P83362; -.
DR CORUM; P83362; -.
DR STRING; 9615.ENSCAFP00000013114; -.
DR PaxDb; P83362; -.
DR Ensembl; ENSCAFT00030009662; ENSCAFP00030008445; ENSCAFG00030005286.
DR Ensembl; ENSCAFT00040036434; ENSCAFP00040031725; ENSCAFG00040019712.
DR Ensembl; ENSCAFT00845052856; ENSCAFP00845041499; ENSCAFG00845029846.
DR GeneID; 476592; -.
DR KEGG; cfa:476592; -.
DR CTD; 28972; -.
DR VEuPathDB; HostDB:ENSCAFG00845029846; -.
DR eggNOG; KOG4112; Eukaryota.
DR GeneTree; ENSGT00390000018321; -.
DR HOGENOM; CLU_134505_1_0_1; -.
DR InParanoid; P83362; -.
DR TreeFam; TF106122; -.
DR Proteomes; UP000002254; Chromosome 20.
DR Bgee; ENSCAFG00000008927; Expressed in adrenal cortex and 48 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005787; C:signal peptidase complex; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR InterPro; IPR037713; Spc1.
DR InterPro; IPR009542; Spc1/SPCS1.
DR PANTHER; PTHR13202; PTHR13202; 1.
DR PANTHER; PTHR13202:SF0; PTHR13202:SF0; 1.
DR Pfam; PF06645; SPC12; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..102
FT /note="Signal peptidase complex subunit 1"
FT /id="PRO_0000215153"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8632014"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:8632014"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8632014"
FT REGION 81..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 102 AA; 11761 MW; EB12830247E532A7 CRC64;
MLEHLSSLPT QMDYKGQKLA EQMFQGIILF SAIVGFIYGY VAEQFGWTVY IVMAGFAFSC
LLTLPPWPIY RRHPLKWLPV QDSGSEDKKP GERKIKRHAK NN
