ID   SC61B_PONAB             Reviewed;          96 AA.
AC   Q5RB31;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Protein transport protein Sec61 subunit beta;
GN   Name=SEC61B;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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). Component of a ribosome-
CC       associated ER translocon complex involved in multi-pass membrane
CC       protein transport into the ER membrane and biogenesis. The SEC61
CC       channel cooperates with the translocating protein TRAM1 to import
CC       nascent proteins into the ER (By similarity). Required for
CC       PKD1/Polycystin-1 biogenesis (By similarity).
CC       {ECO:0000250|UniProtKB:P60468, ECO:0000250|UniProtKB:Q9CQS8}.
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 (By similarity).
CC       The ribosome-associated ER translocon complex includes SEC61A1, SEC61B,
CC       SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147; in the absence
CC       of ribosomes, only the complex forms with NCLN/Nicalin, NOMO and
CC       TMEM147 remains intact (By similarity). Interacts with TRAM1 (By
CC       similarity). {ECO:0000250|UniProtKB:P60467,
CC       ECO:0000250|UniProtKB:P60468}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR858826; CAH91029.1; -; mRNA.
DR   RefSeq; NP_001129010.1; NM_001135538.1.
DR   AlphaFoldDB; Q5RB31; -.
DR   SMR; Q5RB31; -.
DR   STRING; 9601.ENSPPYP00000021785; -.
DR   Ensembl; ENSPPYT00000022675; ENSPPYP00000021785; ENSPPYG00000019441.
DR   GeneID; 100190850; -.
DR   KEGG; pon:100190850; -.
DR   CTD; 10952; -.
DR   eggNOG; KOG3457; Eukaryota.
DR   GeneTree; ENSGT00390000003561; -.
DR   HOGENOM; CLU_133423_4_0_1; -.
DR   InParanoid; Q5RB31; -.
DR   OMA; WGKYTRG; -.
DR   OrthoDB; 1634609at2759; -.
DR   TreeFam; TF313144; -.
DR   Proteomes; UP000001595; Chromosome 9.
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:0005784; C:Sec61 translocon complex; IEA:InterPro.
DR   GO; GO:0048408; F:epidermal growth factor binding; IEA:Ensembl.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:Ensembl.
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   3: Inferred from homology;
KW   Acetylation; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P60468"
FT   CHAIN           2..96
FT                   /note="Protein transport protein Sec61 subunit beta"
FT                   /id="PRO_0000157256"
FT   TOPO_DOM        2..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..96
FT                   /note="Extracellular"
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