SC61B_CANLF
ID SC61B_CANLF Reviewed; 96 AA.
AC P60467; P38390; P38391;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein transport protein Sec61 subunit beta;
GN Name=SEC61B;
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], PROTEIN SEQUENCE OF 2-16; 78-81; 83-86 AND
RP 88-97, SUBUNIT, AND FUNCTION.
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).
RN [2]
RP SUBUNIT.
RX PubMed=10799540; DOI=10.1074/jbc.275.19.14550;
RA Meyer H.-A., Grau H., Kraft R., Kostka S., Prehn S., Kalies K.-U.,
RA Hartmann E.;
RT "Mammalian Sec61 is associated with Sec62 and Sec63.";
RL J. Biol. Chem. 275:14550-14557(2000).
RN [3]
RP SUBUNIT.
RX PubMed=10860986; DOI=10.1073/pnas.97.13.7214;
RA Tyedmers J., Lerner M., Bies C., Dudek J., Skowronek M.H., Haas I.G.,
RA Heim N., Nastainczyk W., Volkmer J., Zimmermann R.;
RT "Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant
RT proteins in dog pancreas microsomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7214-7219(2000).
CC -!- FUNCTION: Component of SEC61 channel-forming translocon complex that
CC mediates transport of signal peptide-containing precursor polypeptides
CC across the 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 Required for PKD1/Polycystin-1 biogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P60468, ECO:0000250|UniProtKB:Q9CQS8,
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
CC (PubMed:10799540, PubMed:10860986, PubMed:8107851). The ribosome-
CC associated ER translocon complex includes SEC61A1, SEC61B, SEC61G,
CC TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147; in the absence of
CC ribosomes, only the complex forms with NCLN/Nicalin, NOMO and TMEM147
CC remains intact (By similarity). Interacts with TRAM1 (By similarity).
CC {ECO:0000250|UniProtKB:P60468, ECO:0000269|PubMed:10799540,
CC ECO:0000269|PubMed:10860986, ECO:0000269|PubMed:8107851}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P60468}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SEC61-beta family. {ECO:0000305}.
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DR EMBL; L25052; AAA19639.1; -; mRNA.
DR PIR; S42409; S42409.
DR RefSeq; NP_001003326.1; NM_001003326.1.
DR PDB; 2WWB; EM; 6.48 A; C=1-96.
DR PDB; 4CG5; EM; 7.40 A; C=61-96.
DR PDB; 4CG6; EM; 7.80 A; C=1-96.
DR PDB; 4CG7; EM; 6.90 A; C=61-96.
DR PDB; 5A6U; EM; 9.00 A; B=61-96.
DR PDB; 6FTG; EM; 9.10 A; z=68-96.
DR PDB; 6FTI; EM; 4.20 A; z=68-96.
DR PDB; 6FTJ; EM; 4.70 A; z=68-96.
DR PDB; 6R7Q; EM; 3.90 A; ZZ=68-96.
DR PDBsum; 2WWB; -.
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 AlphaFoldDB; P60467; -.
DR SMR; P60467; -.
DR BioGRID; 139931; 1.
DR CORUM; P60467; -.
DR IntAct; P60467; 1.
DR MINT; P60467; -.
DR STRING; 9612.ENSCAFP00000003690; -.
DR PaxDb; P60467; -.
DR PRIDE; P60467; -.
DR Ensembl; ENSCAFT00030035555; ENSCAFP00030031011; ENSCAFG00030019313.
DR Ensembl; ENSCAFT00040037323; ENSCAFP00040032525; ENSCAFG00040020183.
DR Ensembl; ENSCAFT00845013672; ENSCAFP00845010616; ENSCAFG00845007765.
DR GeneID; 404018; -.
DR KEGG; cfa:404018; -.
DR CTD; 10952; -.
DR VEuPathDB; HostDB:ENSCAFG00845007765; -.
DR eggNOG; KOG3457; Eukaryota.
DR GeneTree; ENSGT00940000171174; -.
DR HOGENOM; CLU_133423_4_0_1; -.
DR InParanoid; P60467; -.
DR OMA; WGKYTRG; -.
DR OrthoDB; 1634609at2759; -.
DR TreeFam; TF313144; -.
DR Reactome; R-CFA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; P60467; -.
DR Proteomes; UP000002254; Chromosome 11.
DR Bgee; ENSCAFG00000002533; Expressed in pancreas and 47 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:Ensembl.
DR GO; GO:0031205; C:endoplasmic reticulum Sec complex; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005784; C:Sec61 translocon complex; IBA:GO_Central.
DR GO; GO:0048408; F:epidermal growth factor binding; IEA:Ensembl.
DR GO; GO:0015450; F:protein-transporting ATPase activity; TAS:ProtInc.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:Ensembl.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
DR InterPro; IPR030671; Sec61-beta/Sbh.
DR InterPro; IPR016482; SecG/Sec61-beta/Sbh.
DR PANTHER; PTHR13509; PTHR13509; 1.
DR Pfam; PF03911; Sec61_beta; 1.
DR PIRSF; PIRSF006398; Sec61_beta_euk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P60468,
FT ECO:0000269|PubMed:8107851"
FT CHAIN 2..96
FT /note="Protein transport protein Sec61 subunit beta"
FT /id="PRO_0000157253"
FT TOPO_DOM 2..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60468"
FT LIPID 39
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 96 AA; 9974 MW; 5FAFF4197A62FA49 CRC64;
MPGPTPSGTN VGSSGRSPSK AVAARAAGST VRQRKNASCG TRSAGRTTSA GTGGMWRFYT
EDSPGLKVGP VPVLVMSLLF IASVFMLHIW GKYTRS
