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RMR5_ARATH
ID   RMR5_ARATH              Reviewed;         318 AA.
AC   F4HZZ5; Q9LQG6;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Receptor homology region, transmembrane domain- and RING domain-containing protein 5;
DE            Short=AtRMR5;
DE   Flags: Precursor;
GN   Name=RMR5; OrderedLocusNames=At1g35630; ORFNames=F15O4.19;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
CC   -!- FUNCTION: Involved in the trafficking of vacuolar proteins. May
CC       function as a sorting receptor for protein trafficking to the protein
CC       storage vacuole (PSV) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane {ECO:0000250}.
CC       Protein storage vacuole membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF79351.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BX818705; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AC007887; AAF79351.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31820.1; -; Genomic_DNA.
DR   EMBL; BX818705; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; H86477; H86477.
DR   RefSeq; NP_174800.2; NM_103264.3.
DR   AlphaFoldDB; F4HZZ5; -.
DR   SMR; F4HZZ5; -.
DR   STRING; 3702.AT1G35630.1; -.
DR   PaxDb; F4HZZ5; -.
DR   PRIDE; F4HZZ5; -.
DR   EnsemblPlants; AT1G35630.1; AT1G35630.1; AT1G35630.
DR   GeneID; 840463; -.
DR   Gramene; AT1G35630.1; AT1G35630.1; AT1G35630.
DR   KEGG; ath:AT1G35630; -.
DR   Araport; AT1G35630; -.
DR   TAIR; locus:2014726; AT1G35630.
DR   eggNOG; KOG4628; Eukaryota.
DR   HOGENOM; CLU_035275_0_0_1; -.
DR   InParanoid; F4HZZ5; -.
DR   OMA; ICIDDYC; -.
DR   OrthoDB; 1487241at2759; -.
DR   PRO; PR:F4HZZ5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4HZZ5; baseline and differential.
DR   Genevisible; F4HZZ5; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032586; C:protein storage vacuole membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd02123; PA_C_RZF_like; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Metal-binding; Protein transport;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport;
KW   Vacuole; Zinc; Zinc-finger.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..318
FT                   /note="Receptor homology region, transmembrane domain- and
FT                   RING domain-containing protein 5"
FT                   /id="PRO_0000425119"
FT   TOPO_DOM        22..163
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        185..318
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          70..143
FT                   /note="PA"
FT   ZN_FING         233..275
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62..87
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  34916 MW;  6117AFCFF23ABE27 CRC64;
     MNYSWITIMS LLVICKLASA KVVLIGKNTI LSFDDVEATF TPIVRNSGEC GILYVAEPLE
     ACSDITNMAE KRSKYRSSYV LIVLGGCSFE EKVRKAQKAG YKAAIVYNDG YDELLVPMAG
     NSSGVDIHGL LVTRASGEVL KGYADQDEMK LWLIPGFGIS SWSIMGITFI SLLAMSAILA
     TCFVVRRHQI RQSVRDLPHG GQGLSCMPRD LLQSMPTEVY SGVLEESSTS VTCAICIDDY
     CVGEKLRILP CKHKYHAVCI DSWLGRCRSF CPVCKQNPRT GNDVPPASET TPLISPSPNS
     ITSLQSFYDL PIVVRVYL
 
 
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