ID A0A3B3XTS0_9TELE Unreviewed; 408 AA.
AC A0A3B3XTS0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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 Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000018315.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000018315.1}
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; A0A3B3XTS0; -.
DR Ensembl; ENSPMET00000034148.1; ENSPMEP00000018315.1; ENSPMEG00000021290.1.
DR Proteomes; UP000261480; 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 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..72
FT /note="Translocon Sec61/SecY plug"
FT /evidence="ECO:0000259|Pfam:PF10559"
SQ SEQUENCE 408 AA; 44624 MW; C0911B5B81557EB8 CRC64;
MWLTLQKKPF CAVLPEIQKP ERKIQFREKV LWTAITLFIF LVCCQIPLFG IMSSDSADPF
YWMRVILASN RGTLMELGIS PIVTSGLIMQ LLAGAKIIEV GDTPKDRALF NGAQKLFGMI
ITIGQAIVYV MTGMYGDPSE MGAGICLLII IQLFVAGLIV LLLDELLQKG YGLGSGISLF
IATNICETIV WKAFSPTTVN TGRGTEFEGA IIALFHLLAT RTDKVRALRE AFYRQNLPNL
MNLIATVFVF AVVIYFQDTS SGGPARAYPV GGLCYYLSPP ESFGSVLDDP VHAVIYIVFM
LGSCAFFSKT WIEVSGSSAK DVAKQLKEQQ MVMRGHRETS MVHELNRYIP TAAAFGGLCI
GGLSVMADFL GAIGSGTGIL LAVTIIYQYF EIFVKEQSEV GSMGALLF
//
