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ROH1_ARATH
ID   ROH1_ARATH              Reviewed;         415 AA.
AC   Q9CAK4;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Protein ROH1 {ECO:0000303|PubMed:20618910};
GN   Name=ROH1 {ECO:0000303|PubMed:20618910};
GN   OrderedLocusNames=At1g63930 {ECO:0000312|Araport:AT1G63930};
GN   ORFNames=T12P18.5 {ECO:0000312|EMBL:AAG52457.1};
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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH EXO70A1 AND EXO70C1, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=20618910; DOI=10.1111/j.1469-8137.2010.03372.x;
RA   Kulich I., Cole R., Drdova E., Cvrckova F., Soukup A., Fowler J.,
RA   Zarsky V.;
RT   "Arabidopsis exocyst subunits SEC8 and EXO70A1 and exocyst interactor ROH1
RT   are involved in the localized deposition of seed coat pectin.";
RL   New Phytol. 188:615-625(2010).
CC   -!- FUNCTION: Required for seed coat mucilage deposition.
CC       {ECO:0000269|PubMed:20618910}.
CC   -!- SUBUNIT: Interacts with EXO70A1 and EXO70C1.
CC       {ECO:0000269|PubMed:20618910}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in cells expanding in a polar
CC       manner such as pollen and root hairs. {ECO:0000269|PubMed:20618910}.
CC   -!- DISRUPTION PHENOTYPE: Reduced pectin deposition leading to reduced seed
CC       coat mucilage thickness (PubMed:20618910). Characteristic pattern of
CC       pectin deposition to the corners of seed coat volcano cells
CC       (PubMed:20618910). {ECO:0000269|PubMed:20618910}.
CC   -!- MISCELLANEOUS: 'Roh' means corner in Czech.
CC       {ECO:0000305|PubMed:20618910}.
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DR   EMBL; AC010852; AAG52457.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34167.1; -; Genomic_DNA.
DR   EMBL; AK221458; BAD94543.1; -; mRNA.
DR   EMBL; BT023455; AAY56446.1; -; mRNA.
DR   EMBL; BT029011; ABI93920.1; -; mRNA.
DR   PIR; D96664; D96664.
DR   RefSeq; NP_176576.1; NM_105066.3.
DR   AlphaFoldDB; Q9CAK4; -.
DR   IntAct; Q9CAK4; 1.
DR   STRING; 3702.AT1G63930.1; -.
DR   PaxDb; Q9CAK4; -.
DR   PRIDE; Q9CAK4; -.
DR   ProteomicsDB; 177728; -.
DR   EnsemblPlants; AT1G63930.1; AT1G63930.1; AT1G63930.
DR   GeneID; 842696; -.
DR   Gramene; AT1G63930.1; AT1G63930.1; AT1G63930.
DR   KEGG; ath:AT1G63930; -.
DR   Araport; AT1G63930; -.
DR   TAIR; locus:2195513; AT1G63930.
DR   eggNOG; ENOG502QUJZ; Eukaryota.
DR   HOGENOM; CLU_060027_0_0_1; -.
DR   InParanoid; Q9CAK4; -.
DR   OMA; LVRHWQK; -.
DR   OrthoDB; 1150244at2759; -.
DR   PhylomeDB; Q9CAK4; -.
DR   PRO; PR:Q9CAK4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9CAK4; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048354; P:mucilage biosynthetic process involved in seed coat development; IMP:TAIR.
DR   GO; GO:0010214; P:seed coat development; IMP:TAIR.
DR   InterPro; IPR008511; ROH1-like.
DR   Pfam; PF05633; BPS1; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..415
FT                   /note="Protein ROH1"
FT                   /id="PRO_0000448861"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          184..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   415 AA;  45637 MW;  0BA156C38E9AAE70 CRC64;
     MRPAQDNQGS FLGRISIRRN QFVDVNNEQE QEDLELFQKH IADRFTELLS PPQPPPSDEI
     NTVASVAATE QIMSVTWLRK LMDVFLCCEA EFKAILLMGR DPTQISKPPF DRLVPEMLDR
     SIKALDICTA VVNGIDSVRH YQRLAEIAVT ALEQRPLGDG NVRRAKRALA NLVVALSLED
     KENVSGGGGG GGGGNKTTER SWSFGRRSGG SSAASKGGAT IGQLKSSSWA VGRNWSAAKQ
     IHAMTANLTP PRGNEAAGLP QPMFIMSTVM VFVMWVLTAA VPCQERSGLA NHLPVPPKHL
     NWAQSLIGIH EKIGDEWKKK EKKGSAGLME EMTRMEKLGH SLMEFADGFH YPAEKDAAES
     AAVQVAEMAE ICRRMEEELV PLQQQIREVF HRIVRSRAEI LEVLEQAGKV SAPVV
 
 
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