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SC61A_BORSA
ID   SC61A_BORSA             Reviewed;         476 AA.
AC   Q8AY33;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Protein transport protein Sec61 subunit alpha;
GN   Name=sec61a;
OS   Boreogadus saida (Polar cod) (Gadus saida).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Boreogadus.
OX   NCBI_TaxID=44932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=12771183; DOI=10.1242/jcs.00597;
RA   Romisch K., Collie N., Soto N., Logue J., Lindsay M., Scheper W.,
RA   Cheng C.-H.C.;
RT   "Protein translocation across the endoplasmic reticulum membrane in cold-
RT   adapted organisms.";
RL   J. Cell Sci. 116:2875-2883(2003).
CC   -!- FUNCTION: Plays a crucial role in the insertion of secretory and
CC       membrane polypeptides into the ER. Required for assembly of membrane
CC       and secretory proteins. Tightly associated with membrane-bound
CC       ribosomes, either directly or through adapter proteins (By similarity).
CC       Plays a role in pronephric kidney tubule development (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P61620}.
CC   -!- SUBUNIT: Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and
CC       SEC61-gamma. {ECO:0000250}.
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; AY103474; AAM52490.1; -; mRNA.
DR   AlphaFoldDB; Q8AY33; -.
DR   SMR; Q8AY33; -.
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:0039019; P:pronephric nephron development; 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   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..476
FT                   /note="Protein transport protein Sec61 subunit alpha"
FT                   /id="PRO_0000131799"
FT   TOPO_DOM        2..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..76
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..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..240
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..288
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        310..354
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        355..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        376..420
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        442..445
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        463..476
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   476 AA;  52302 MW;  70EFEFE62AAAE684 CRC64;
     MGIKFLEVIK PFCAVLPEIQ KPERKIQFRE KVLWTAITLF IFLVCCQIPL FGIMSSDSAD
     PFYWMRVILA SNRGTLMELG ISPIVTSDLI MQLLAGAKII EVGDSPKDRA LFNGAQKLFG
     MIITIGQAIV YVMTGMYGDP SEMGAGICLV IIIQLFVAGL IVLLLDELLQ KGYGLGSGIS
     LLIATNICET IVWKAFSPTT VNTGRGTEFE GAIIALFHLL ATRTDKVRAL REAFYRQNLP
     NLMNLIATVF VFAVVIYFQG FRVDLPIKSA RYRGQYNTYP IKLFYTSNIP IILQSALVSN
     LYVISQMLST RFSGNFIVNL LGTWSDTSTG GPARAYPVGG LCYFLSPPES FGSVLDDPVH
     AAIYIVFMLG SCAFFSKTWI EVSGSSAKDV AKQLKEQQMV MRGHRETSMV HELNRYIPTA
     AAFGGLCIGG LSVMADFLGA IGSGTGILLA VTIIYQYFEI FVKEQSEMGS MGGLFF
 
 
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