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3.A.19.1.1
The ATP hydrolysis-dependent TRC receptor TRC40 (Asna-1) (Stefanovic and Hegde, 2007). (TRC40 is homologous to the ArsA ATPase of E. coli (TC# 3.A.4.1.1) and the GET3 ATPase of yeast (TC# 8.A.26.1.1)) Loss yields embryonic lethality. Tryptophan-rich basic protein (WRB) is the tail-anchored (TA) protein insertion receptor. Also called congenital heart disease protein-5 (CHD5). Related to the yeast Get1 protein in 3.A.21.1.1. Calcium-modulating cyclophilin ligand (CAML) is a mammal-specific receptor for TRC40, an ATPase targeting newly synthesized TA proteins.  CAML mediates membrane insertion of TA proteins.  TRC40 (Asna1) has been shown to mediate membrane insertion of two proteins, RAMP4 and Sec61beta, without the participation of other cytosolic proteins by a mechanism that depends on the presence of ATP or ADP and a protease-sensitive receptor in the ER membrane (Favaloro et al. 2010).  TRC40 is required for release of Herpes simplex virus 1 (HSV1) virions (Ott et al. 2016). The functions and reciprocal interactions of the two subunits of the heteromeric TRC40 recpeptor, WBR and CAML (CAMLG), have revealed mutual dependencies for stability; CAML seems to normally be present in 5-fold excess over WBR (Colombo et al. 2016). CAMLG interacts with Classical Swine Fever Virus (CSFV) p7 and mediates calcium permeability in the ER (Gladue et al. 2018).

Accession Number:O43681
Protein Name:Arsenical pump-driving ATPase aka TRC40
Length:348
Molecular Weight:38793.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate tail-anchored proteins

Cross database links:

Genevestigator: O43681
eggNOG: prNOG15894
HEGENOM: HBG646947
RefSeq: NP_004308.2   
Entrez Gene ID: 439   
Drugbank: Drugbank Link   
OMIM: 601913  gene
KEGG: hsa:439   

Gene Ontology

GO:0005783 C:endoplasmic reticulum
GO:0005730 C:nucleolus
GO:0005625 C:soluble fraction
GO:0015105 F:arsenite transmembrane transporter activity
GO:0005524 F:ATP binding
GO:0016787 F:hydrolase activity
GO:0046872 F:metal ion binding
GO:0006875 P:cellular metal ion homeostasis
GO:0006810 P:transport

References (10)

[1] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[2] “The DNA sequence and biology of human chromosome 19.”  Grimwood J.et.al.   15057824
[3] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[4] “Isolation of the ATP-binding human homolog of the arsA component of the bacterial arsenite transporter.”  Kurdi-Haidar B.et.al.   8884272
[5] “Biochemical characterization of the human arsenite-stimulated ATPase (hASNA-I).”  Kurdi-Haidar B.et.al.   9712828
[6] “Dual cytoplasmic and nuclear distribution of the novel arsenite-stimulated human ATPase (hASNA-I).”  Kurdi-Haidar B.et.al.   9736449
[7] “Immunohistochemical analysis of the distribution of the human ATPase (hASNA-I) in normal tissues and its overexpression in breast adenomas and carcinomas.”  Kurdi-Haidar B.et.al.   9774623
[8] “Identification of a targeting factor for posttranslational membrane protein insertion into the ER.”  Stefanovic S.et.al.   17382883
[9] “Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.”  Favaloro V.et.al.   18477612
[10] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330

External Searches:

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FASTA formatted sequence
1:	MAAGVAGWGV EAEEFEDAPD VEPLEPTLSN IIEQRSLKWI FVGGKGGVGK TTCSCSLAVQ 
61:	LSKGRESVLI ISTDPAHNIS DAFDQKFSKV PTKVKGYDNL FAMEIDPSLG VAELPDEFFE 
121:	EDNMLSMGKK MMQEAMSAFP GIDEAMSYAE VMRLVKGMNF SVVVFDTAPT GHTLRLLNFP 
181:	TIVERGLGRL MQIKNQISPF ISQMCNMLGL GDMNADQLAS KLEETLPVIR SVSEQFKDPE 
241:	QTTFICVCIA EFLSLYETER LIQELAKCKI DTHNIIVNQL VFPDPEKPCK MCEARHKIQA 
301:	KYLDQMEDLY EDFHIVKLPL LPHEVRGADK VNTFSALLLE PYKPPSAQ