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S61A1_PONAB
ID   S61A1_PONAB             Reviewed;         476 AA.
AC   Q5R5L5; Q5R785; Q5R9P8;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Protein transport protein Sec61 subunit alpha isoform 1;
DE            Short=Sec61 alpha-1;
GN   Name=SEC61A1; Synonyms=SEC61A;
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). Forms a ribosome receptor and a
CC       gated pore in the ER membrane, both functions required for
CC       cotranslational translocation of nascent polypeptides. May cooperate
CC       with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable post-
CC       translational transport of small presecretory proteins. Component of a
CC       ribosome-associated ER translocon complex involved in multi-pass
CC       membrane protein transport into the ER membrane and biogenesis. The
CC       SEC61 channel cooperates with the translocating protein TRAM1 to import
CC       nascent proteins into the ER. Controls the passive efflux of calcium
CC       ions from the ER lumen to the cytosol through SEC61 channel,
CC       contributing to the maintenance of cellular calcium homeostasis (By
CC       similarity). Plays a critical role in nephrogenesis, specifically at
CC       pronephros stage (By similarity). {ECO:0000250|UniProtKB:P61619,
CC       ECO:0000250|UniProtKB:P61620}.
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). {ECO:0000250|UniProtKB:P38377,
CC       ECO:0000250|UniProtKB:P61619}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P61619}; Multi-pass membrane protein
CC       {ECO:0000305}. Note=Localizes exclusively in granular structures in the
CC       endoplasmic reticulum (ER). {ECO:0000250|UniProtKB:P61619}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR   EMBL; CR859335; CAH91512.1; -; mRNA.
DR   EMBL; CR860233; CAH92375.1; -; mRNA.
DR   EMBL; CR860842; CAH92951.1; -; mRNA.
DR   RefSeq; NP_001126739.1; NM_001133267.1.
DR   AlphaFoldDB; Q5R5L5; -.
DR   SMR; Q5R5L5; -.
DR   STRING; 9601.ENSPPYP00000015030; -.
DR   Ensembl; ENSPPYT00000015631; ENSPPYP00000015030; ENSPPYG00000013438.
DR   GeneID; 100173741; -.
DR   KEGG; pon:100173741; -.
DR   CTD; 29927; -.
DR   eggNOG; KOG1373; Eukaryota.
DR   GeneTree; ENSGT00390000003721; -.
DR   HOGENOM; CLU_031763_2_0_1; -.
DR   InParanoid; Q5R5L5; -.
DR   OMA; VIEDPMH; -.
DR   OrthoDB; 482911at2759; -.
DR   TreeFam; TF300348; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005262; F:calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0006613; P:cotranslational protein targeting to membrane; ISS:UniProtKB.
DR   GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISS:UniProtKB.
DR   GO; GO:0039019; P:pronephric nephron development; ISS:UniProtKB.
DR   GO; GO:0045048; P:protein insertion into ER membrane; ISS:UniProtKB.
DR   GO; GO:0045047; P:protein targeting to ER; ISS:UniProtKB.
DR   Gene3D; 1.10.3370.10; -; 1.
DR   InterPro; IPR002208; SecY/SEC61-alpha.
DR   InterPro; IPR030659; SecY_CS.
DR   InterPro; IPR023201; SecY_dom_sf.
DR   InterPro; IPR019561; Translocon_Sec61/SecY_plug_dom.
DR   PANTHER; PTHR10906; PTHR10906; 1.
DR   Pfam; PF10559; Plug_translocon; 1.
DR   Pfam; PF00344; SecY; 1.
DR   PIRSF; PIRSF004557; SecY; 1.
DR   SUPFAM; SSF103491; SSF103491; 1.
DR   TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR   PROSITE; PS00755; SECY_1; 1.
DR   PROSITE; PS00756; SECY_2; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Endoplasmic reticulum; Membrane; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..476
FT                   /note="Protein transport protein Sec61 subunit alpha
FT                   isoform 1"
FT                   /id="PRO_0000131793"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..75
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..117
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..144
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..172
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        194..202
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        221..240
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..288
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..476
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        344
FT                   /note="Y -> H (in Ref. 1; CAH91512)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  52265 MW;  44A9B7B37C7C82E4 CRC64;
     MAIKFLEVIK PFCVILPEIQ KPERKIQFKE KVLWTAITLF IFLVCCQIPL FGIMSSDSAD
     PFYWMRVILA SNRGTLMELG ISPIVTSGLI MQLLAGAKII EVGDTPKDRA LFNGAQKLFG
     MIITIGQSIV YVMTGMYGDP SEMGAGICLL ITIQLFVAGL IVLLLDELLQ KGYGLGSGIS
     LFIATNICET IVWKAFSPTT VNTGRGMEFE GAIIALFHLL ATRTDKVRAL REAFYRQNLP
     NLMNLIATIF VFAVVIYFQG FRVDLPIKSA RYRGQYNTYP IKLFYTSNIP IILQSALVSN
     LYVISQMLSA RFSGNLLVSL LGTWSDTSSG GPARAYPVGG LCYYLSPPES FGSVLEDPVH
     AVVYIVFMLG SCAFFSKTWI EVSGSSAKDV AKQLKEQQMV MRGHRETSMV HELNRYIPTA
     AAFGGLCIGA LSVLADFLGA IGSGTGILLA VTIIYQYFEI FVKEQSEVGS MGALLF
 
 
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