ID A0A3B5AXY9_9TELE Unreviewed; 410 AA.
AC A0A3B5AXY9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Protein transport protein SEC61 subunit alpha {ECO:0000256|ARBA:ARBA00014282};
DE AltName: Full=Protein transport protein Sec61 subunit alpha {ECO:0000256|ARBA:ARBA00019838};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000026223.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000026223.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. The SEC61
CC channel is also involved in ER membrane insertion of transmembrane
CC proteins: it mediates membrane insertion of the first few transmembrane
CC segments of proteins, while insertion of subsequent transmembrane
CC regions of multi-pass membrane proteins is mediated by the multi-pass
CC translocon (MPT) complex. {ECO:0000256|ARBA:ARBA00034676}.
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 SEC61 channel associates with the multi-pass translocon (MPT)
CC complex. {ECO:0000256|ARBA:ARBA00034794}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003484}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003484}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family.
CC {ECO:0000256|ARBA:ARBA00005751, ECO:0000256|RuleBase:RU004349}.
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DR AlphaFoldDB; A0A3B5AXY9; -.
DR Ensembl; ENSSPAT00000026651.1; ENSSPAP00000026223.1; ENSSPAG00000019746.1.
DR GeneTree; ENSGT00390000003721; -.
DR Proteomes; UP000261400; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3370.10; SecY subunit domain; 2.
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:SF19; PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT ALPHA ISOFORM 1; 1.
DR PANTHER; PTHR10906; SECY/SEC61-ALPHA FAMILY MEMBER; 1.
DR Pfam; PF10559; Plug_translocon; 1.
DR Pfam; PF00344; SecY; 2.
DR PIRSF; PIRSF004557; SecY; 2.
DR SUPFAM; SSF103491; Preprotein translocase SecY subunit; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU003484};
KW Translocation {ECO:0000256|ARBA:ARBA00023010,
KW ECO:0000256|RuleBase:RU003484};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003484};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003484}.
FT TRANSMEM 32..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..74
FT /note="Translocon Sec61/SecY plug"
FT /evidence="ECO:0000259|Pfam:PF10559"
SQ SEQUENCE 410 AA; 44768 MW; 8CDECC9A24A58041 CRC64;
MGIKFLEVIK PFCAVLPEIQ KPERKIQFRE KVLWTAITLF IFLVCCQIPL FGIMSSDSAD
PFYWMRVILA SNRGTLMELG ISPIVTSGLI MQLLAGAKII EVGDTPKDRA LFNGAQKLFG
MIITIGQAIV YVMTGMYGDP SEMGAGICLL IIIQLFVAGL IVLLLDELLQ KGYGLGSGIS
LFIATNICET IVWKAFSPTT VNTGRGTEFE GAIIALFHLL ATRTDKVRAL REAFYRQNLP
NLMNLIATVF VFAVVIYFQD TSSGGPARAY PVGGLCYYLS PPESFGSVLE DPVHAVIYIV
FMLGSCAFFS KTWIEVSGSS AKDVAKQLKE QQMVMRGHRE TSMVHELNRY IPTAAAFGGL
CIGGLSVMAD FLGAIGSGTG ILLAVTIIYQ YFEIFVKEQS EVGSMGALLF
//
