ID A0A445B4X9_ARAHY Unreviewed; 475 AA.
AC A0A445B4X9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Reticulon-like protein {ECO:0000256|RuleBase:RU363132};
GN ORFNames=Ahy_A10g048297 {ECO:0000313|EMBL:RYR33676.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR33676.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR33676.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR33676.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU363132}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the 3-beta-HSD family.
CC {ECO:0000256|ARBA:ARBA00009219}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RYR33676.1}.
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DR EMBL; SDMP01000010; RYR33676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445B4X9; -.
DR Proteomes; UP000289738; Chromosome a10.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003388; Reticulon.
DR PANTHER; PTHR43245; BIFUNCTIONAL POLYMYXIN RESISTANCE PROTEIN ARNA; 1.
DR PANTHER; PTHR43245:SF51; SHORT CHAIN DEHYDROGENASE_REDUCTASE FAMILY 42E, MEMBER 2; 1.
DR Pfam; PF01073; 3Beta_HSD; 1.
DR Pfam; PF02453; Reticulon; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU363132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363132};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363132}.
FT TRANSMEM 308..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT TRANSMEM 400..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT DOMAIN 295..475
FT /note="Reticulon"
FT /evidence="ECO:0000259|PROSITE:PS50845"
SQ SEQUENCE 475 AA; 53020 MW; 359F29CB04E64A4E CRC64;
MAAPNSSINN YQLHHSVNVQ GTQNVIDACV QLRVKRLVYT SSSSVVFDGV HGIHNGKESM
PYPPKHNDHY SATKAQGEAL VLKANGTSGI LTCSLRPSSI FGPGDRLMVP SSVDAAKAGK
TKFIIGDGNN MYDFTYVGNV AHSHLCADRA LASEGEVSKK AAGEAYFITN MEPIKFWEFM
SLILEGLGYE RPRIKIPAFV LMPIALLVEY TYKLLGPYGM KVPQLTPSRV RLLSCNRTFD
CSKAKERLGY EPIVTLKEGL RRTIDSFSHL RAENQLKPKR EGPSKASVYL GSGRVADTLL
WKDRKRTITT LLVLIAIYLS FIEPGNTFIT ALSKLLLFVS IFLFIHGILP AKVLGYTVQK
MPKSWFHLSE DMSHQLAVSV VSVWNIPMNV LKSLAQGNEW MLFFKVVFSL LLLSFFGAFS
LQNLYKIGLT TAFIAFYIYE KKEEEIDDLF IKALSFGCKL KSDAIRKFLP SKKSE
//