SH3P1_ARATH
ID SH3P1_ARATH Reviewed; 439 AA.
AC Q9C865;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=SH3 domain-containing protein 1 {ECO:0000312|EMBL:AAL32438.1};
GN Name=SH3P1; OrderedLocusNames=At1g31440 {ECO:0000312|Araport:AT1G31440};
GN ORFNames=T8E3.10 {ECO:0000312|EMBL:AAG51264.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH AUXI1.
RX PubMed=11701884; DOI=10.2307/3871590;
RA Lam B.C.-H., Sage T.L., Bianchi F., Blumwald E.;
RT "Role of SH3 domain-containing proteins in clathrin-mediated vesicle
RT trafficking in Arabidopsis.";
RL Plant Cell 13:2499-2512(2001).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Lipid binding protein bound strongly to phosphatidic acid,
CC phosphatidylinositol-4-phosphate and phosphatidylinositol-4,5-
CC bisphosphate. Binds actin in vitro. Involved in trafficking and
CC modification of clathrin-coated vesicles.
CC {ECO:0000269|PubMed:11701884}.
CC -!- SUBUNIT: Interacts with the auxilin-like protein AUXI1.
CC {ECO:0000269|PubMed:11701884}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:11701884}. Cell membrane
CC {ECO:0000269|PubMed:11701884}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:11701884}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:11701884}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:11701884}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers. Detected in seedlings,
CC roots, leaves and stems. {ECO:0000269|PubMed:11701884}.
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DR EMBL; AF367773; AAL32438.1; -; mRNA.
DR EMBL; AC027135; AAG51264.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31356.1; -; Genomic_DNA.
DR EMBL; AY080835; AAL87310.1; -; mRNA.
DR EMBL; AY113984; AAM45032.1; -; mRNA.
DR PIR; D86440; D86440.
DR RefSeq; NP_174429.1; NM_102883.5.
DR AlphaFoldDB; Q9C865; -.
DR SMR; Q9C865; -.
DR IntAct; Q9C865; 2.
DR STRING; 3702.AT1G31440.1; -.
DR iPTMnet; Q9C865; -.
DR MetOSite; Q9C865; -.
DR PaxDb; Q9C865; -.
DR PRIDE; Q9C865; -.
DR ProteomicsDB; 234509; -.
DR EnsemblPlants; AT1G31440.1; AT1G31440.1; AT1G31440.
DR GeneID; 840034; -.
DR Gramene; AT1G31440.1; AT1G31440.1; AT1G31440.
DR KEGG; ath:AT1G31440; -.
DR Araport; AT1G31440; -.
DR TAIR; locus:2206174; AT1G31440.
DR eggNOG; ENOG502QU26; Eukaryota.
DR HOGENOM; CLU_045749_0_0_1; -.
DR InParanoid; Q9C865; -.
DR OMA; HSEMILE; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q9C865; -.
DR PRO; PR:Q9C865; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C865; baseline and differential.
DR Genevisible; Q9C865; AT.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Golgi apparatus; Membrane; Reference proteome; SH3 domain.
FT CHAIN 1..439
FT /note="SH3 domain-containing protein 1"
FT /id="PRO_0000434150"
FT DOMAIN 32..263
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 366..425
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 277..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 49258 MW; 41A42B784BE8AC25 CRC64;
MEAIRKQAAK LREQVARQQQ AVLKHLGHVN ADAVVVDEEE LHCHQKLQDL YSSTKAAKRL
QRNIVRGLEG FIATGTKVVE IGLKFAEDFK KYGDENPDAN TPLSRVAHHF GTSYKSVEGE
RETLLGVLSE QVCEPIRTMI YSAPLEDARH LVNHYDRLRQ EVEAQATDVL RRRSKLKESD
ISEEAYIKLK NSESRLAELK SSMKTLGKEA TKAMLEVDDQ QQNVTSQRLR ALVEAERSYH
RNALDILDKL HSEMIAEEEA IGSSPKSLPL HIEDSASLPQ QEPNSNSSGE IKSNPLGKIK
ASRREEIKSN PQEVTKPSPK DEMKSSPQEE TKSNHQKEIK SSPQEEIKKS NGSDDHHNHQ
LLSQNDSYFL AKVVHPFDAQ APGELSLAVD DYVIVRQVAG TGWSEGEYKG KAGWFPSAYV
EKQEKAPASK IVESNSKQQ
