ID A8XMU5_CAEBR Unreviewed; 255 AA.
AC A8XMU5;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Protein CBG15874 {ECO:0000313|EMBL:CAP33971.2};
GN Name=hrg-2.1 {ECO:0000313|WormBase:CBG15874};
GN ORFNames=CBG15874 {ECO:0000313|EMBL:CAP33971.2,
GN ECO:0000313|WormBase:CBG15874}, CBG_15874
GN {ECO:0000313|EMBL:CAP33971.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP33971.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP33971.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP33971.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- SIMILARITY: Belongs to the FAX family. {ECO:0000256|ARBA:ARBA00006475}.
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DR EMBL; HE600911; CAP33971.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XMU5; -.
DR EnsemblMetazoa; CBG15874.1; CBG15874.1; WBGene00035987.
DR WormBase; CBG15874; CBP26243; WBGene00035987; Cbr-hrg-2.1.
DR eggNOG; KOG4244; Eukaryota.
DR HOGENOM; CLU_044137_1_0_1; -.
DR InParanoid; A8XMU5; -.
DR OMA; YCERVKT; -.
DR OrthoDB; 3684737at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd03080; GST_N_Metaxin_like; 1.
DR InterPro; IPR026928; FAX/IsoI-like.
DR InterPro; IPR033468; Metaxin_GST.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12289:SF40; CADMIUM-INDUCIBLE LYSOSOMAL PROTEIN CDR-5; 1.
DR PANTHER; PTHR12289; METAXIN RELATED; 1.
DR Pfam; PF17171; GST_C_6; 1.
DR Pfam; PF17172; GST_N_4; 1.
DR SFLD; SFLDG01180; SUF1; 1.
DR SFLD; SFLDG01200; SUF1.1; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..147
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17172"
FT DOMAIN 208..249
FT /note="Metaxin glutathione S-transferase"
FT /evidence="ECO:0000259|Pfam:PF17171"
SQ SEQUENCE 255 AA; 29136 MW; 2ACE2BE6E4268CE2 CRC64;
MILEIIAIII IVLYLLKLIF WIFKTFFTTP SVPSTPKIHK PDFQKDVVYL YQFPRTNTVP
NLSSYCLKIE TFLRAFKIPH EIIETPSLRS RNGTLPFVEL NGEHIPDSDL IETKLREHFH
VPNLAPELEA QATAISRLVD NHLLGLIVKY KASEEGWYDA LLRGVPGPNF LKTILRPIIK
KLFMSKVHAR VGLSIGSFTE EETELLCHKD LVAVQNSIRG KFLFGDKITS ADCAVFGEVA
SAYYPFPNKF QKNYR
//
