SEC63_PONAB
ID SEC63_PONAB Reviewed; 761 AA.
AC Q5R660;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translocation protein SEC63 homolog;
GN Name=SEC63;
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 cotranslational and post-translational transport of
CC certain precursor polypeptides across endoplasmic reticulum (ER).
CC Proposed to play an auxiliary role in recognition of precursors with
CC short and apolar signal peptides. May cooperate with SEC62 and
CC HSPA5/BiP to facilitate targeting of small presecretory proteins into
CC the SEC61 channel-forming translocon complex, triggering channel
CC opening for polypeptide translocation to the ER lumen (By similarity).
CC Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to
CC the plasma membrane of the primary cilia (By similarity).
CC {ECO:0000250|UniProtKB:Q8VHE0, ECO:0000250|UniProtKB:Q9UGP8}.
CC -!- SUBUNIT: The ER translocon complex consists of channel-forming core
CC components SEC61A1, SEC61B and SEC61G and different auxiliary
CC components such as SEC62 and SEC63. {ECO:0000250|UniProtKB:P82008}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
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DR EMBL; CR860636; CAH92756.1; -; mRNA.
DR RefSeq; NP_001126607.1; NM_001133135.1.
DR AlphaFoldDB; Q5R660; -.
DR STRING; 9601.ENSPPYP00000018910; -.
DR PRIDE; Q5R660; -.
DR GeneID; 100173604; -.
DR KEGG; pon:100173604; -.
DR CTD; 11231; -.
DR eggNOG; KOG0721; Eukaryota.
DR HOGENOM; CLU_014210_1_0_1; -.
DR InParanoid; Q5R660; -.
DR OrthoDB; 686427at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISS:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR027137; Sec63.
DR InterPro; IPR004179; Sec63-dom.
DR PANTHER; PTHR24075:SF0; PTHR24075:SF0; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF02889; Sec63; 2.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Coiled coil; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..761
FT /note="Translocation protein SEC63 homolog"
FT /id="PRO_0000292660"
FT TOPO_DOM 1..14
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..188
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..761
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..165
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 197..542
FT /note="SEC63 1"
FT DOMAIN 638..715
FT /note="SEC63 2"
FT REGION 492..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 598..636
FT /evidence="ECO:0000255"
FT COMPBIAS 520..536
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..761
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 538
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP8"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP8"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP8"
SQ SEQUENCE 761 AA; 88125 MW; 26ABD433CA0AA529 CRC64;
MAGQQFQYDD SGNTFFYFLT SFVGLIVIPA TYYLWPRDQN AEQIRLKNIR KVYGRCMWYR
LRLLKPQPNI IPTVKKIVLL AGWALFLFLA YKVSKTDREY QEYNPYEVLN LDPGATVAEI
KKQYRLLSLK YHPDKGGDEV MFMRIAKAYA ALTDEESRKN WEEFGNPDGP QATSFGIALP
AWIVDQKNSI LVLLVYGLAF MVILPVVVGS WWYRSIRYSG DQILIRTTQI YTYFVYKTRN
MDMKRLIMVL AGASEFDPQY NKDATSRPTD NILIPQLIRE IGSINLKKNE PPLTCPYSLK
ARVLLLSHLA RMKIPETLEE DQQFMLKKCP ALLQEMVNVI CQLIVMARNR EEREFRAPTL
ASLENCMKLS QMAVQGLQQF KSPLLQLPHI EEDNLRRVSN HKKYKIKTIQ DLVSLKESDR
HTLLHFLEDE KYEEVMAVLG SFPYVTMDIK SQVLDDEDSN NITVGSLVTV LVKLTRQTMA
EVFEKEQSIC AAEEQPAEDG QGETNKNRTK GGWQQKSKGP KKTAKSKKKK KPLKKKPTPV
LLPQSKQQKQ KQANGVVGNE AAVKEDEEEV SDKGSDSEEE ETNRDSQSEK DDGSDRDSDR
EQDEKQNKDD EAEWQELQQS IQRKERALLE TKSKITHPVY SLYFPEEKQE WWWLYIADRK
EQTLISMPYH VCTLKDTEEV ELKFPAPGKP GNYQYTVFLR SDSYMGLDQI KPLKLEVHEA
KPVPENHPQW DTAIEGDEDQ EDSEGFEDSF EEEEEEEEDD D
