S61A2_DANRE
ID S61A2_DANRE Reviewed; 476 AA.
AC Q90YL4; Q7ZUL2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein transport protein Sec61 subunit alpha-like 2;
GN Name=sec61al2; Synonyms=sec61ab, sec61b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hartmann E.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Appears to play a crucial role in the insertion of secretory
CC and membrane polypeptides into the ER. It is required for assembly of
CC membrane and secretory proteins. Found to be tightly associated with
CC membrane-bound ribosomes, either directly or through adaptor proteins
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and
CC SEC61-gamma. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AY034614; AAK61394.1; -; mRNA.
DR EMBL; BC048881; AAH48881.1; -; mRNA.
DR RefSeq; NP_963871.1; NM_201577.1.
DR AlphaFoldDB; Q90YL4; -.
DR SMR; Q90YL4; -.
DR STRING; 7955.ENSDARP00000049424; -.
DR PaxDb; Q90YL4; -.
DR GeneID; 266796; -.
DR KEGG; dre:266796; -.
DR CTD; 266796; -.
DR ZFIN; ZDB-GENE-021016-2; sec61a1l.
DR eggNOG; KOG1373; Eukaryota.
DR InParanoid; Q90YL4; -.
DR OrthoDB; 482911at2759; -.
DR PhylomeDB; Q90YL4; -.
DR TreeFam; TF300348; -.
DR PRO; PR:Q90YL4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0048793; P:pronephros development; IMP:ZFIN.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
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-like
FT 2"
FT /id="PRO_0000131798"
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 CONFLICT 129
FT /note="V -> I (in Ref. 1; AAK61394)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52368 MW; 7EC5EF07FDB63A8B CRC64;
MAIKFLEVIK PFCAVLPEIQ KPERRIQFKE KVLWTAITLF IFLVCCQIPL FGIMSSDSAD
PFYWMRVIMA SNRGTLMELG ISPIVTSGLI MQLLAGAKII EVGDTPKDRA LFNGAQKLFG
MIITIGQAVV YVMTGMYGDP SEMGAGICLL IIIQLFVAGL IVLLLDELLQ KGYGLGSGIS
LFIATNICET IVWKAFSPTT VNTGRGTEFE GAIIALFHLL ATRTDKVRAL REAFYRQNLP
NLMNLIATIF VFAVVIYFQG FRVDLPIKSA RYRGQYNTYP IKLFYTSNIP IILQSALVSN
LYVISQMLST RFSGNFLVNL LGTWSDTSTG GPARAYPVGG LCYYLSPPES FGTVLEDPIH
AIIYIIFMLG SCAFFSKTWI EVSGSSAKDV AKQLKEQQMV MRGHRETSMV HELNRYIPTA
AAFGGLCIGG LSVMADFLGA IGSGTGILLA VTIIYQYFEI FVKEQSEVGS VGALLF
