ID   SEC62_PONAB             Reviewed;         399 AA.
AC   Q5R4Q3; Q5NVB7;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Translocation protein SEC62;
DE   AltName: Full=Translocation protein 1;
DE            Short=TP-1;
GN   Name=SEC62; Synonyms=TLOC1;
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=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates post-translational transport of precursor
CC       polypeptides across endoplasmic reticulum (ER). Proposed to act as a
CC       targeting receptor for small presecretory proteins containing short and
CC       apolar signal peptides. Targets and properly positions newly
CC       synthesized presecretory proteins into the SEC61 channel-forming
CC       translocon complex, triggering channel opening for polypeptide
CC       translocation to the ER lumen. {ECO:0000250|UniProtKB:Q99442}.
CC   -!- SUBUNIT: The ER translocon complex that consists of channel-forming
CC       core components SEC61A1, SEC61B and SEC61G and different auxiliary
CC       components such as SEC62 and SEC63. Interacts with SEC61B.
CC       {ECO:0000250|UniProtKB:P82009, ECO:0000250|UniProtKB:Q99442}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SEC62 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI29746.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR861192; CAH93263.1; -; mRNA.
DR   EMBL; CR926121; CAI29746.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001127648.1; NM_001134176.1.
DR   AlphaFoldDB; Q5R4Q3; -.
DR   SMR; Q5R4Q3; -.
DR   STRING; 9601.ENSPPYP00000015966; -.
DR   Ensembl; ENSPPYT00000016605; ENSPPYP00000015966; ENSPPYG00000014285.
DR   GeneID; 100174729; -.
DR   KEGG; pon:100174729; -.
DR   CTD; 7095; -.
DR   eggNOG; KOG2927; Eukaryota.
DR   GeneTree; ENSGT00390000002757; -.
DR   HOGENOM; CLU_051910_0_0_1; -.
DR   InParanoid; Q5R4Q3; -.
DR   OMA; HQEQSFN; -.
DR   OrthoDB; 1474000at2759; -.
DR   TreeFam; TF314944; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISS:UniProtKB.
DR   InterPro; IPR004728; Sec62.
DR   PANTHER; PTHR12443; PTHR12443; 1.
DR   Pfam; PF03839; Sec62; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..399
FT                   /note="Translocation protein SEC62"
FT                   /id="PRO_0000206618"
FT   TOPO_DOM        1..196
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        218..234
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..399
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          108..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..388
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         158
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99442"
FT   MOD_RES         341
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99442"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99442"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99442"
FT   MOD_RES         375
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99442"
FT   CONFLICT        137
FT                   /note="K -> KK (in Ref. 1; CAI29746)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="I -> V (in Ref. 1; CAI29746)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   399 AA;  45888 MW;  D848BFD7ACBD0A55 CRC64;
     MAERRRHKKR IQEVGEPSKE EKAVAKYLRF NCPTKSTNMM GHRVDYFIAS KAVDCLLDSK
     WAKAKKGEEA LFTTRESVVD YCNRLLKKQF FHRALKVMKM KYDKDIKKEK DKGKAESGKE
     EDKKSKKENI KDEKTKKEKE KKKDGEKEDS KKEETPGTPK KKETKKKFKL EPHDDQVFLD
     GNEVYVWIYD PVHFKTFVMG LILVIAVIAA TLFPLWPAEM RVGVYYLSVG AGCFVASILL
     LAVARCILFL IIWLITGGRH HFWFLPNLTA DVGFIDSFRP LYTHEYKGPK ADLKKDEKSE
     TKKQQKSDSE EKSDSEKKED EEGKVGPGNH GTEGLGGERH SDTDSDRRED DRSQHSSGNG
     NDFEMITKEE LEQQTDGDCE EEEEEENDGE TPKSSHEKS