S61A1_CANLF
ID S61A1_CANLF Reviewed; 476 AA.
AC P38377;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein transport protein Sec61 subunit alpha isoform 1;
DE Short=Sec61 alpha-1;
GN Name=SEC61A1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-20, AND SUBUNIT.
RX PubMed=1423609; DOI=10.1016/0092-8674(92)90517-g;
RA Goerlich D., Prehn S., Hartmann E., Kalies K.-U., Rapoport T.A.;
RT "A mammalian homolog of SEC61p and SECYp is associated with ribosomes and
RT nascent polypeptides during translocation.";
RL Cell 71:489-503(1992).
RN [2]
RP SUBUNIT.
RX PubMed=10799540; DOI=10.1074/jbc.275.19.14550;
RA Meyer H.-A., Grau H., Kraft R., Kostka S., Prehn S., Kalies K.-U.,
RA Hartmann E.;
RT "Mammalian Sec61 is associated with Sec62 and Sec63.";
RL J. Biol. Chem. 275:14550-14557(2000).
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
CC (PubMed:10799540, PubMed:1423609). The ribosome-associated ER
CC translocon complex includes SEC61A1, SEC61B, SEC61G, TMCO1, CCDC47,
CC NCLN/Nicalin, NOMO and TMEM147; in the absence of ribosomes, only the
CC complex forms with NCLN/Nicalin, NOMO and TMEM147 remains intact (By
CC similarity). {ECO:0000250|UniProtKB:P61619,
CC ECO:0000269|PubMed:10799540, ECO:0000269|PubMed:1423609}.
CC -!- INTERACTION:
CC P38377; P62161: Calm3; Xeno; NbExp=4; IntAct=EBI-8517797, EBI-397530;
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; M96629; AAA30891.1; -; mRNA.
DR PIR; A44170; A44170.
DR RefSeq; NP_001003315.1; NM_001003315.1.
DR PDB; 2WWB; EM; 6.48 A; A=1-476.
DR PDB; 3JC2; EM; 3.60 A; 1=1-476.
DR PDB; 4CG5; EM; 7.40 A; A=1-476.
DR PDB; 4CG6; EM; 7.80 A; A=1-476.
DR PDB; 4CG7; EM; 6.90 A; A=1-476.
DR PDB; 5A6U; EM; 9.00 A; A=26-476.
DR PDB; 6FTG; EM; 9.10 A; x=5-465.
DR PDB; 6FTI; EM; 4.20 A; x=5-465.
DR PDB; 6FTJ; EM; 4.70 A; x=5-465.
DR PDB; 6R7Q; EM; 3.90 A; XX=5-465.
DR PDB; 6Z3T; EM; 2.69 A; A=1-476.
DR PDBsum; 2WWB; -.
DR PDBsum; 3JC2; -.
DR PDBsum; 4CG5; -.
DR PDBsum; 4CG6; -.
DR PDBsum; 4CG7; -.
DR PDBsum; 5A6U; -.
DR PDBsum; 6FTG; -.
DR PDBsum; 6FTI; -.
DR PDBsum; 6FTJ; -.
DR PDBsum; 6R7Q; -.
DR PDBsum; 6Z3T; -.
DR AlphaFoldDB; P38377; -.
DR SMR; P38377; -.
DR CORUM; P38377; -.
DR IntAct; P38377; 1.
DR MINT; P38377; -.
DR STRING; 9615.ENSCAFP00000061198; -.
DR PaxDb; P38377; -.
DR PRIDE; P38377; -.
DR GeneID; 404006; -.
DR KEGG; cfa:404006; -.
DR CTD; 29927; -.
DR eggNOG; KOG1373; Eukaryota.
DR InParanoid; P38377; -.
DR OrthoDB; 482911at2759; -.
DR EvolutionaryTrace; P38377; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005784; C:Sec61 translocon complex; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Direct protein sequencing;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1423609"
FT CHAIN 2..476
FT /note="Protein transport protein Sec61 subunit alpha
FT isoform 1"
FT /id="PRO_0000131790"
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"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:6Z3T"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:6Z3T"
FT TURN 61..69
FT /evidence="ECO:0007829|PDB:6Z3T"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 110..132
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 179..193
FT /evidence="ECO:0007829|PDB:6Z3T"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:6Z3T"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:6Z3T"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 247..259
FT /evidence="ECO:0007829|PDB:6Z3T"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:6Z3T"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 289..312
FT /evidence="ECO:0007829|PDB:6Z3T"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 358..380
FT /evidence="ECO:0007829|PDB:6Z3T"
FT TURN 381..384
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:6Z3T"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:6Z3T"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:6Z3T"
FT TURN 415..418
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:6Z3T"
FT TURN 434..439
FT /evidence="ECO:0007829|PDB:6Z3T"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:6Z3T"
FT HELIX 446..463
FT /evidence="ECO:0007829|PDB:6Z3T"
SQ SEQUENCE 476 AA; 52239 MW; B1A9B7A6697327FE 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 LCHYLSPPES FGSVLEDPVH
AVVYIVFMLG SCAFFSKTWI EVSGSSAKDV AKQLKEQQMV MRGHRETSMV HELNRYIPTA
AAFGGLCIGA LSVLADFLGA IGSGTGILLA VTIIYQYFEI FVKEQSEVGS MGALLF
