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SC61G_CANLF
ID   SC61G_CANLF             Reviewed;          68 AA.
AC   P60058; P38384;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Protein transport protein Sec61 subunit gamma;
GN   Name=SEC61G;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBUNIT, FUNCTION,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=Cocker spaniel; TISSUE=Kidney;
RX   PubMed=8107851; DOI=10.1038/367654a0;
RA   Hartmann E., Sommer T., Prehn S., Goerlich D., Jentsch S., Rapoport T.A.;
RT   "Evolutionary conservation of components of the protein translocation
RT   complex.";
RL   Nature 367:654-657(1994).
CC   -!- FUNCTION: Component of SEC61 channel-forming translocon complex that
CC       mediates transport of signal peptide-containing precursor polypeptides
CC       across endoplasmic reticulum (ER) (PubMed:8107851). Component of a
CC       ribosome-associated ER translocon complex involved in multi-pass
CC       membrane protein transport into the ER membrane and biogenesis (By
CC       similarity). The SEC61 channel cooperates with the translocating
CC       protein TRAM1 to import nascent proteins into the ER (By similarity).
CC       {ECO:0000250|UniProtKB:P60059, ECO:0000250|UniProtKB:P61619,
CC       ECO:0000269|PubMed:8107851}.
CC   -!- SUBUNIT: The SEC61 channel-forming translocon complex consists of
CC       channel-forming core components SEC61A1, SEC61B and SEC61G and
CC       different auxiliary components such as SEC62 and SEC63 (PubMed:8107851)
CC       (Probable). The ribosome-associated ER translocon complex includes
CC       SEC61A1, SEC61B, SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147;
CC       in the absence of ribosomes, only the complex forms with NCLN/Nicalin,
CC       NOMO and TMEM147 remains intact (By similarity).
CC       {ECO:0000250|UniProtKB:P60059, ECO:0000269|PubMed:8107851,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:8107851}; Single-pass membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000305}.
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DR   EMBL; L25086; AAA19705.1; -; mRNA.
DR   RefSeq; NP_001003325.1; NM_001003325.1.
DR   PDB; 2WWB; EM; 6.48 A; B=1-68.
DR   PDB; 3JC2; EM; 3.60 A; 2=7-68.
DR   PDB; 4CG5; EM; 7.40 A; B=1-68.
DR   PDB; 4CG6; EM; 7.80 A; B=1-68.
DR   PDB; 4CG7; EM; 6.90 A; B=1-68.
DR   PDB; 5A6U; EM; 9.00 A; G=7-68.
DR   PDB; 6FTG; EM; 9.10 A; y=7-68.
DR   PDB; 6FTI; EM; 4.20 A; y=7-68.
DR   PDB; 6FTJ; EM; 4.70 A; y=7-68.
DR   PDB; 6R7Q; EM; 3.90 A; YY=7-68.
DR   PDB; 6Z3T; EM; 2.69 A; B=1-68.
DR   PDBsum; 2WWB; -.
DR   PDBsum; 3JC2; -.
DR   PDBsum; 4CG5; -.
DR   PDBsum; 4CG6; -.
DR   PDBsum; 4CG7; -.
DR   PDBsum; 5A6U; -.
DR   PDBsum; 6FTG; -.
DR   PDBsum; 6FTI; -.
DR   PDBsum; 6FTJ; -.
DR   PDBsum; 6R7Q; -.
DR   PDBsum; 6Z3T; -.
DR   AlphaFoldDB; P60058; -.
DR   SMR; P60058; -.
DR   CORUM; P60058; -.
DR   STRING; 9612.ENSCAFP00000005144; -.
DR   PaxDb; P60058; -.
DR   Ensembl; ENSCAFT00000104631; ENSCAFP00000074802; ENSCAFG00000057055.
DR   Ensembl; ENSCAFT00030012384; ENSCAFP00030010835; ENSCAFG00030006723.
DR   Ensembl; ENSCAFT00040013857; ENSCAFP00040012002; ENSCAFG00040007446.
DR   Ensembl; ENSCAFT00845020063; ENSCAFP00845015721; ENSCAFG00845011317.
DR   GeneID; 404017; -.
DR   KEGG; cfa:404017; -.
DR   CTD; 23480; -.
DR   VEuPathDB; HostDB:ENSCAFG00845011317; -.
DR   eggNOG; KOG3498; Eukaryota.
DR   GeneTree; ENSGT00390000001319; -.
DR   HOGENOM; CLU_167752_2_0_1; -.
DR   InParanoid; P60058; -.
DR   OMA; RDGNQFL; -.
DR   OrthoDB; 1623399at2759; -.
DR   TreeFam; TF300232; -.
DR   Reactome; R-CFA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   EvolutionaryTrace; P60058; -.
DR   Proteomes; UP000002254; Chromosome 18.
DR   Bgee; ENSCAFG00000003459; Expressed in saliva-secreting gland 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; NAS:UniProtKB.
DR   GO; GO:0071261; C:Ssh1 translocon complex; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; IMP:CAFA.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IGI:UniProtKB.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0022406; P:membrane docking; IMP:CAFA.
DR   GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR   GO; GO:0045047; P:protein targeting to ER; IGI:UniProtKB.
DR   DisProt; DP00117; -.
DR   Gene3D; 1.20.5.820; -; 1.
DR   HAMAP; MF_00422; SecE; 1.
DR   InterPro; IPR023391; Prot_translocase_SecE_dom_sf.
DR   InterPro; IPR008158; Translocase_Sec61-g.
DR   InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR   Pfam; PF00584; SecE; 1.
DR   SUPFAM; SSF103456; SSF103456; 1.
DR   TIGRFAMs; TIGR00327; secE_euk_arch; 1.
DR   PROSITE; PS01067; SECE_SEC61G; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..68
FT                   /note="Protein transport protein Sec61 subunit gamma"
FT                   /id="PRO_0000104194"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..68
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P60059"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60059"
FT   HELIX           9..22
FT                   /evidence="ECO:0007829|PDB:6Z3T"
FT   HELIX           32..64
FT                   /evidence="ECO:0007829|PDB:6Z3T"
SQ   SEQUENCE   68 AA;  7741 MW;  14C8279A22548561 CRC64;
     MDQVMQFVEP SRQFVKDSIR LVKRCTKPDR KEFQKIAMAT AIGFAIMGFI GFFVKLIHIP
     INNIIVGG
 
 
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