ID A0A0S3SDD1_PHAAN Unreviewed; 579 AA.
AC A0A0S3SDD1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Reticulon-like protein {ECO:0000256|RuleBase:RU363132};
GN Name=Vigan.06G213800 {ECO:0000313|EMBL:BAT90849.1};
GN ORFNames=VIGAN_06213800 {ECO:0000313|EMBL:BAT90849.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT90849.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT90849.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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}.
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DR EMBL; AP015039; BAT90849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3SDD1; -.
DR Proteomes; UP000291084; Chromosome 6.
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:UP000291084};
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 397..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT TRANSMEM 425..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT TRANSMEM 514..532
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT DOMAIN 385..576
FT /note="Reticulon"
FT /evidence="ECO:0000259|PROSITE:PS50845"
SQ SEQUENCE 579 AA; 65763 MW; 43FA66A35F20CE35 CRC64;
MTVDDRFAHL NPKTCVVVGG RGFLGRSLVL RLLKLGNWIV RIADSAHSLQ FHHSESILAQ
ALSSARASYF HIDLTDKCNI VKVLGGSSVV FFMDVAGVDV NDFYTCYRLI VQGAKNVISA
CRECRVKRLI YNSSADVVFD GLHDIRDGDE SLAYPWKTDN MLSDLKAQAE SLILSVNDID
GLLTCSLRPS NVFGPGDTEF VPYFLKSARY GFTKFIIGTG DNLSDFTFSE NVTHAHICAE
EALNFQTVSV AGKAFFITNN EPIEFWEFLS LLLEGLGYRR PYVKLPAKLA QYILSVLKWS
HEKLGSRYFS YPLLVHFFQL ASYTRTFNCT KAHKHIGYSP IVSLEEGVTL TIESFSYLSK
DSCLSRSFSS TEQSKADKLL GGGKVADILL WRDEKKSFTY FVVLVLLFYW FFLSGRTFIS
SAAKLLLLAT LLFYGHGFLP SKLFGFNIQR IPLSCFEISD AVVKDSVITT VYLWNKGFQI
IRRLAHGEDW SAFFKIAVFL YLMKIFLSKL LTKLIGIGLV FAFMGFFVYE QYESEIDGMV
DVLFTSLKEF MIYLMRISPV FKSRLLRYHD NFQRYEKNG
//
