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SPCS3_CHICK
ID   SPCS3_CHICK             Reviewed;         180 AA.
AC   P28687;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Signal peptidase complex subunit 3;
DE   AltName: Full=Microsomal signal peptidase 22/23 kDa subunit;
DE            Short=SPC22/23;
DE            Short=SPase 22/23 kDa subunit;
DE   AltName: Full=gp23;
GN   Name=SPCS3 {ECO:0000305}; Synonyms=SPC22 {ECO:0000303|PubMed:2831945};
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT
RP   ASN-141.
RC   TISSUE=Oviduct;
RX   PubMed=1546959; DOI=10.1042/bj2820447;
RA   Newsome A.L., McLean J.W., Lively M.O.;
RT   "Molecular cloning of a cDNA encoding the glycoprotein of hen oviduct
RT   microsomal signal peptidase.";
RL   Biochem. J. 282:447-452(1992).
RN   [2]
RP   IDENTIFICATION IN THE SIGNAL PEPTIDASE COMPLEX, AND TISSUE SPECIFICITY.
RX   PubMed=2831945; DOI=10.1021/bi00400a010;
RA   Baker R.K., Lively M.O.;
RT   "Purification and characterization of hen oviduct microsomal signal
RT   peptidase.";
RL   Biochemistry 26:8561-8567(1987).
CC   -!- FUNCTION: Essential component of the signal peptidase complex (SPC)
CC       which catalyzes the cleavage of N-terminal signal sequences from
CC       nascent proteins as they are translocated into the lumen of the
CC       endoplasmic reticulum (By similarity). Essential for the SPC catalytic
CC       activity, possibly by stabilizing and positioning the active center of
CC       the complex close to the lumenal surface (By similarity).
CC       {ECO:0000250|UniProtKB:P61009, ECO:0000250|UniProtKB:Q12133}.
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:2831945). 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:2831945). 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. This ensures the selectivity of the
CC       complex towards h-regions shorter than 18-20 amino acids (By
CC       similarity). {ECO:0000250|UniProtKB:P61009,
CC       ECO:0000269|PubMed:2831945}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P61008}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:P61008}.
CC   -!- TISSUE SPECIFICITY: Expressed in hen oviduct (at protein level).
CC       {ECO:0000269|PubMed:2831945}.
CC   -!- SIMILARITY: Belongs to the SPCS3 family. {ECO:0000305}.
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DR   EMBL; X60795; CAA43208.1; -; mRNA.
DR   PIR; S22412; S22412.
DR   RefSeq; NP_990628.1; NM_205297.1.
DR   AlphaFoldDB; P28687; -.
DR   SMR; P28687; -.
DR   STRING; 9031.ENSGALP00000017599; -.
DR   MEROPS; X45.001; -.
DR   iPTMnet; P28687; -.
DR   PaxDb; P28687; -.
DR   Ensembl; ENSGALT00000017620; ENSGALP00000017599; ENSGALG00000010839.
DR   GeneID; 396234; -.
DR   KEGG; gga:396234; -.
DR   CTD; 60559; -.
DR   VEuPathDB; HostDB:geneid_396234; -.
DR   eggNOG; KOG3372; Eukaryota.
DR   GeneTree; ENSGT00390000009223; -.
DR   InParanoid; P28687; -.
DR   OMA; FGCFVTT; -.
DR   OrthoDB; 1514162at2759; -.
DR   PhylomeDB; P28687; -.
DR   PRO; PR:P28687; -.
DR   Proteomes; UP000000539; Chromosome 4.
DR   Bgee; ENSGALG00000010839; Expressed in granulocyte and 13 other tissues.
DR   ExpressionAtlas; P28687; baseline and differential.
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; IPR007653; SPC3.
DR   PANTHER; PTHR12804; PTHR12804; 1.
DR   Pfam; PF04573; SPC22; 1.
DR   PIRSF; PIRSF016089; SPC22; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..180
FT                   /note="Signal peptidase complex subunit 3"
FT                   /id="PRO_0000218941"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P61008"
FT   TRANSMEM        12..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..180
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:P61008"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:1546959"
SQ   SEQUENCE   180 AA;  20230 MW;  A5572439EB8210AA CRC64;
     MNTVLSRANS LFAFSLSVMA ALTFGCFITT AFKERSVPVS IAVSRVTLRN VEDFTGPRER
     SDLAFVTFDI TADLQSIFDW NVKQLFLYLS AEYSTKNNAL NQVVLWDKII LRGDNPRLFL
     KDMKSKYFFF DDGNGLKGNR NVTLTLSWNV VPNAGLLPLV TGSGHMSVPF PDTYETTKSY
 
 
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