ID H9G869_ANOCA Unreviewed; 213 AA.
AC H9G869;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Signal peptidase complex subunit 2 {ECO:0000256|ARBA:ARBA00017057, ECO:0000256|RuleBase:RU368033};
GN Name=SPCS2 {ECO:0000313|Ensembl:ENSACAP00000003775.3};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000003775.3, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000003775.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000003775.3};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000003775.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. Enhances the enzymatic activity of SPC and facilitates the
CC interactions between different components of the translocation site.
CC {ECO:0000256|RuleBase:RU368033}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368033}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU368033}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SPCS2 family.
CC {ECO:0000256|ARBA:ARBA00007324, ECO:0000256|RuleBase:RU368033}.
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DR RefSeq; XP_008118894.1; XM_008120687.2.
DR AlphaFoldDB; H9G869; -.
DR STRING; 28377.ENSACAP00000003775; -.
DR Ensembl; ENSACAT00000003867.4; ENSACAP00000003775.3; ENSACAG00000003877.4.
DR GeneID; 100558372; -.
DR KEGG; acs:100558372; -.
DR CTD; 9789; -.
DR eggNOG; KOG4072; Eukaryota.
DR GeneTree; ENSGT00440000038181; -.
DR HOGENOM; CLU_094622_0_0_1; -.
DR InParanoid; H9G869; -.
DR OrthoDB; 2903540at2759; -.
DR TreeFam; TF314545; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000003877; Expressed in hemipenis and 13 other cell types or tissues.
DR GO; GO:0005787; C:signal peptidase complex; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-UniRule.
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; MICROSOMAL SIGNAL PEPTIDASE 25 KDA SUBUNIT; 1.
DR PANTHER; PTHR13085:SF0; SIGNAL PEPTIDASE COMPLEX SUBUNIT 2; 1.
DR Pfam; PF06703; SPC25; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU368033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368033};
KW Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368033}.
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368033"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368033"
SQ SEQUENCE 213 AA; 23798 MW; 1745B03C70283DC3 CRC64;
MAAKGSGGCA GGGGGGANKN GILDKWKIED KPVKVDKWDG SAVKNSLDDS AKKVLLEKYK
YVENFCLIDG RLIICTISCL FAIVALIWDY LHPFPESKPV LAVCVVSYFV MMGILTIYTS
YKEKSIFLVA HRKDPAGMDP DDIWQLSSSL KRFDDKYTLK MTFISGRTKQ QREAEFTKSI
AKFFDDNGTL VMEAFEPEVS KLHDSLLTEK KTK
//
