ID W2T127_NECAM Unreviewed; 719 AA.
AC W2T127;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 28-JAN-2026, entry version 45.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog {ECO:0000256|ARBA:ARBA00070663};
GN ORFNames=NECAME_03861 {ECO:0000313|EMBL:ETN74946.1};
OS Necator americanus (Human hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC Necator.
OX NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN74946.1, ECO:0000313|Proteomes:UP000053676};
RN [1] {ECO:0000313|Proteomes:UP000053676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441737; DOI=10.1038/ng.2875;
RA Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT "Genome of the human hookworm Necator americanus.";
RL Nat. Genet. 46:261-269(2014).
CC -!- FUNCTION: May function as a proteasomal ubiquitin receptor. May promote
CC the deubiquitinating activity associated with the 26S proteasome.
CC {ECO:0000256|ARBA:ARBA00054744}.
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ADRM1 family.
CC {ECO:0000256|ARBA:ARBA00009216}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. 17-beta-HSD 3 subfamily. {ECO:0000256|ARBA:ARBA00038261}.
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DR EMBL; KI660323; ETN74946.1; -; Genomic_DNA.
DR AlphaFoldDB; W2T127; -.
DR STRING; 51031.W2T127; -.
DR KEGG; nai:NECAME_03861; -.
DR OrthoDB; 5545019at2759; -.
DR Proteomes; UP000053676; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030497; P:fatty acid elongation; IEA:TreeGrafter.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd05356; 17beta-HSD1_like_SDR_c; 1.
DR CDD; cd13314; PH_Rpn13; 1.
DR FunFam; 2.30.29.70:FF:000001; Proteasomal ubiquitin receptor ADRM1; 1.
DR FunFam; 3.40.50.720:FF:000467; Steroid dehydrogenase 4; 1.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.30.29.70; Proteasomal ubiquitin receptor Rpn13/ADRM1; 1.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43086:SF2; HYDROXYSTEROID DEHYDROGENASE-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR43086; VERY-LONG-CHAIN 3-OXOOACYL-COA REDUCTASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF04683; Rpn13_ADRM1_Pru; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51917; PRU; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053676};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955}.
FT DOMAIN 15..134
FT /note="Pru"
FT /evidence="ECO:0000259|PROSITE:PS51917"
FT DOMAIN 263..374
FT /note="DEUBAD"
FT /evidence="ECO:0000259|PROSITE:PS51916"
FT REGION 147..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..256
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..392
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 77684 MW; A7FB9A1C7FAB8FE8 CRC64;
MSAMFSTSRS SQGGSSSGNL IEFKAGRSFL QPAAAINKKK VVADKTKGLV FIKQSNDQLM
HFCWKNRETG AIVDDLIIFP GDTEFKEVKG CPDGKVYMLK FKTSDERRLF WIQDGNNDAD
KDLCQKVGKL METLQCSYQR EIYQVNDALN KPPTTRASAR GGSSERTTGG LSTANLAGLS
GSEELGALGG LDQQQLMQLL QFMNQGSSDS PALVSQIPSG NNTDRNTSSG APKVSASELT
QLQTLLGGLR TPGTRGADSS QGSSERQVAV ELGDIVAGGQ VVETAKNNAD RLLNHMPAED
KSSSDTKKAL EDTVRSPHYR QAANTFGHAL STGQMAPVLE RFGISDGAAQ AAASGNLLEF
AKKLTEAERG GDVPEESSEP AAAANAESTS APEGEEVVKE PKPKRMMPCD CLFVTAGYCT
VAFAAYKIGI AVFNILWPYV IRTPVDLHEK AGAKWAVVTG ATDGIGRGYA YELARKGFNI
FLVSRSQSKL DETNKGICEK YDKVEVRTFA FDFCAGSVEA YKPLLNALNA VEVGVLINNV
GMSYEYPENL HKVEGGLERI GAITTINTLP PTILSASLLE QMLLRKKGVI VNISSSASYN
PMALWAVYSA TKKYVNWLTE ILRMEYTNSG IIFQTICPMM VATKMSKVHK TSFFTPSAES
FAASAVRTIG LVSETSGFLS HQIQIEAMNL MPAALVNRLT TKFSVAIREA ALRKKMKTQ
//
