SRC2_ARATH
ID SRC2_ARATH Reviewed; 324 AA.
AC O04023; O81814;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Protein SRC2 homolog {ECO:0000305};
DE Short=AtSRC2 {ECO:0000303|PubMed:16227454};
GN Name=SRC2 {ECO:0000303|PubMed:16227454};
GN OrderedLocusNames=At1g09070 {ECO:0000312|Araport:AT1G09070};
GN ORFNames=F7G19.6 {ECO:0000312|EMBL:AAB70401.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=10216258; DOI=10.1016/s0378-1119(99)00073-6;
RA Aubourg S., Picaud A., Kreis M., Lecharny A.;
RT "Structure and expression of three src2 homologues and a novel subfamily of
RT flavoprotein monooxygenase genes revealed by the analysis of a 25kb
RT fragment from Arabidopsis thaliana chromosome IV.";
RL Gene 230:197-205(1999).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=16227454; DOI=10.1105/tpc.105.035212;
RA Oufattole M., Park J.H., Poxleitner M., Jiang L., Rogers J.C.;
RT "Selective membrane protein internalization accompanies movement from the
RT endoplasmic reticulum to the protein storage vacuole pathway in
RT Arabidopsis.";
RL Plant Cell 17:3066-3080(2005).
RN [6]
RP FUNCTION, INTERACTION WITH RBOHF, SUBCELLULAR LOCATION, AND INDUCTION BY
RP COLD STRESS.
RX PubMed=23872431; DOI=10.1016/j.bbamcr.2013.06.024;
RA Kawarazaki T., Kimura S., Iizuka A., Hanamata S., Nibori H., Michikawa M.,
RA Imai A., Abe M., Kaya H., Kuchitsu K.;
RT "A low temperature-inducible protein AtSRC2 enhances the ROS-producing
RT activity of NADPH oxidase AtRbohF.";
RL Biochim. Biophys. Acta 1833:2775-2780(2013).
CC -!- FUNCTION: May act as an activator of the calcium-dependent activation
CC of RBOHF that mediates reactive oxygen species (ROS) production and may
CC play a role in cold responses. {ECO:0000269|PubMed:23872431}.
CC -!- SUBUNIT: Interacts with RBOHF (via N-terminus).
CC {ECO:0000269|PubMed:23872431}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16227454}; Single-pass type II membrane protein
CC {ECO:0000255}. Protein storage vacuole membrane
CC {ECO:0000269|PubMed:16227454}; Single-pass type II membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:23872431}; Single-pass
CC type II membrane protein {ECO:0000255}. Note=Binds to C-terminal
CC sequence of alpha-TIP and moves from the ER to vacuoles. Movement is
CC accompanied by membrane internalization, and SRC2 is present in
CC crystalloid-like structures within protein storage vacuoles (PSVs) in
CC mature seeds. {ECO:0000269|PubMed:16227454}.
CC -!- INDUCTION: By cold stress in roots. {ECO:0000269|PubMed:16227454}.
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DR EMBL; AJ007586; CAA07573.1; -; mRNA.
DR EMBL; AC000106; AAB70401.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28391.1; -; Genomic_DNA.
DR EMBL; AY045580; AAK73938.1; -; mRNA.
DR EMBL; AY142027; AAM98291.1; -; mRNA.
DR PIR; G86222; G86222.
DR PIR; T51602; T51602.
DR RefSeq; NP_563835.1; NM_100778.3.
DR AlphaFoldDB; O04023; -.
DR SMR; O04023; -.
DR STRING; 3702.AT1G09070.1; -.
DR iPTMnet; O04023; -.
DR PaxDb; O04023; -.
DR PRIDE; O04023; -.
DR ProteomicsDB; 226720; -.
DR EnsemblPlants; AT1G09070.1; AT1G09070.1; AT1G09070.
DR GeneID; 837428; -.
DR Gramene; AT1G09070.1; AT1G09070.1; AT1G09070.
DR KEGG; ath:AT1G09070; -.
DR Araport; AT1G09070; -.
DR TAIR; locus:2036004; AT1G09070.
DR eggNOG; ENOG502QUNY; Eukaryota.
DR HOGENOM; CLU_049673_1_0_1; -.
DR InParanoid; O04023; -.
DR OMA; AYGKPQK; -.
DR OrthoDB; 1277586at2759; -.
DR PhylomeDB; O04023; -.
DR PRO; PR:O04023; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04023; baseline and differential.
DR Genevisible; O04023; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0000326; C:protein storage vacuole; IDA:TAIR.
DR GO; GO:0032586; C:protein storage vacuole membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0006623; P:protein targeting to vacuole; TAS:TAIR.
DR CDD; cd04051; C2_SRC2_like; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR044750; C2_SRC2/BAP.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Membrane; Reference proteome;
KW Signal-anchor; Stress response; Transmembrane; Transmembrane helix;
KW Vacuole.
FT CHAIN 1..324
FT /note="Protein SRC2 homolog"
FT /id="PRO_0000433973"
FT TOPO_DOM 1..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16227454"
FT TRANSMEM 280..300
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..324
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16227454"
FT DOMAIN 1..111
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 141..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..257
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 197
FT /note="D -> G (in Ref. 1; CAA07573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 34189 MW; B946DA1E4C6D8B9E CRC64;
MECRSLDLTI ISAEDLKDVQ LIGKQDLYAV VSINGDARTK QKTKVDKDCG TKPKWKHQMK
LTVDDAAARD NRLTLVFEIV ADRPIAGDKP VGEVSVPVKE LLDQNKGDEE KTVTYAVRLP
NGKAKGSLKF SFKFGEKYTY GSSSGPHAPV PSAMDHKTMD QPVTAYPPGH GAPSAYPAPP
AGPSSGYPPQ GHDDKHDGVY GYPQQAGYPA GTGGYPPPGA YPQQGGYPGY PPQQQGGYPG
YPPQGPYGYP QQGYPPQGPY GYPQQQAHGK PQKPKKHGKA GAGMGLGLGL GAGLLGGLLV
GEAVSDIADM GDMGDMGDMG GFDF
