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Database: UniProt
Entry: A0A3P8TIR4_AMPPE
LinkDB: A0A3P8TIR4_AMPPE
Original site: A0A3P8TIR4_AMPPE 
ID   A0A3P8TIR4_AMPPE        Unreviewed;       390 AA.
AC   A0A3P8TIR4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-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   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000024536.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000024536.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000024536.1}
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; A0A3P8TIR4; -.
DR   STRING; 161767.ENSAPEP00000024536; -.
DR   Ensembl; ENSAPET00000025180.1; ENSAPEP00000024536.1; ENSAPEG00000017426.1.
DR   GeneTree; ENSGT00390000003721; -.
DR   OMA; RDNSMIR; -.
DR   Proteomes; UP000265080; Chromosome 6.
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; 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   NCBIfam; TIGR00967; 3a0501s007; 1.
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; 1.
DR   PIRSF; PIRSF004557; SecY; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000265080};
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        24..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        234..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..66
FT                   /note="Translocon Sec61/SecY plug"
FT                   /evidence="ECO:0000259|Pfam:PF10559"
SQ   SEQUENCE   390 AA;  43134 MW;  2C53829317D54701 CRC64;
     MFPFCAVLPE IQKPERKIQF REKVLWTAIT LFIFLVCCQI PLFGIMSSDS ADPFYWMRVI
     LASNRGTLME LGISPIVTSG LIMQLLAGAK IIEVGDTPKD RALFNGAQKL FGMIITIGQA
     IVYVMTGMYG DPSEMGAGIC LLIIIQLFVA GLIVLLLDEL LQKGYGLGSG ISLFIATNIC
     ETIVWKAFSP TTVNTGRGTE FEGAIIALFH LLATRTDKVR ALREAFYRQN LPNLMNLIAT
     VFVFAVVIYF QGFRVDLPIK SARYRGQYNT YPIKLFYTSN IPIILQSALV SNLYVISQML
     STRFSGNFLV NLLGTWSDTS SGGPARAYPV GGLCYYLSPP ESFGSVLEDP VHALIYIFFM
     LGSCAFFSKT WIEVSGSSAK DVTHNCFLFS
//
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