Search Results

Overview

Uniprot ID	P61619
Protein Name	Protein transport protein Sec61 subunit alpha isoform 1
Gene Name	SEC61A1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
107	IEVGDTPKDRALFNG

Function

Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (PubMed:12475939, PubMed:22375059, PubMed:28782633, PubMed:29719251, PubMed:32814900). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (PubMed:22375059, PubMed:28782633, PubMed:29719251). May cooperate with auxiliary protein SEC62, SEC63 and HSPA5/BiP to enable post-translational transport of small presecretory proteins (PubMed:22375059, PubMed:29719251). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (PubMed:32820719, PubMed:36261522). The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER (PubMed:8616892). Controls the passive efflux of calcium ions from the ER lumen to the cytosol through SEC61 channel, contributing to the maintenance of cellular calcium homeostasis (PubMed:28782633). Plays a critical role in nephrogenesis, specifically at pronephros stage (By similarity)

Protein Sequence

10 MAIKFLEVIK 20 PFCVILPEIQ 30 KPERKIQFKE 40 KVLWTAITLF 50 IFLVCCQIPL 60 FGIMSSDSAD 70 PFYWMRVILA 80 SNRGTLMELG 90 ISPIVTSGLI 100 MQLLAGAKII 110 EVGDTPKDRA 120 LFNGAQKLFG 130 MIITIGQSIV 140 YVMTGMYGDP 150 SEMGAGICLL 160 ITIQLFVAGL 170 IVLLLDELLQ 180 KGYGLGSGIS 190 LFIATNICET 200 IVWKAFSPTT 210 VNTGRGMEFE 220 GAIIALFHLL 230 ATRTDKVRAL 240 REAFYRQNLP 250 NLMNLIATIF 260 VFAVVIYFQG 270 FRVDLPIKSA 280 RYRGQYNTYP 290 IKLFYTSNIP 300 IILQSALVSN 310 LYVISQMLSA 320 RFSGNLLVSL 330 LGTWSDTSSG 340 GPARAYPVGG 350 LCYYLSPPES 360 FGSVLEDPVH 370 AVVYIVFMLG 380 SCAFFSKTWI 390 EVSGSSAKDV 400 AKQLKEQQMV 410 MRGHRETSMV 420 HELNRYIPTA 430 AAFGGLCIGA 440 LSVLADFLGA 450 IGSGTGILLA 460 VTIIYQYFEI 470 FVKEQSEVGS MGALLF

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005783	endoplasmic reticulum
Cellular Component	GO:0005789	endoplasmic reticulum membrane
Cellular Component	GO:0016020	membrane
Cellular Component	GO:0005784	Sec61 translocon complex
Molecular Function	GO:0005262	calcium channel activity
Molecular Function	GO:0008320	protein transmembrane transporter activity
Molecular Function	GO:0043022	ribosome binding
Molecular Function	GO:0005048	signal sequence binding
Biological Process	GO:0006613	cotranslational protein targeting to membrane
Biological Process	GO:0007029	endoplasmic reticulum organization
Biological Process	GO:0006620	post-translational protein targeting to endoplasmic reticulum membrane
Biological Process	GO:0031204	post-translational protein targeting to membrane, translocation
Biological Process	GO:0039019	pronephric nephron development
Biological Process	GO:0045048	protein insertion into ER membrane
Biological Process	GO:0045047	protein targeting to ER
Biological Process	GO:0034341	response to type II interferon
Biological Process	GO:0006614	SRP-dependent cotranslational protein targeting to membrane
Biological Process	GO:0006616	SRP-dependent cotranslational protein targeting to membrane, translocation

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.