SH3P3_ARATH
ID SH3P3_ARATH Reviewed; 351 AA.
AC Q8L7W0; Q8W5A0; Q9SVW5;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=SH3 domain-containing protein 3 {ECO:0000303|PubMed:11701884};
DE Short=AtSH3P3 {ECO:0000303|PubMed:11701884};
GN Name=SH3P3 {ECO:0000303|PubMed:11701884};
GN OrderedLocusNames=At4g18060 {ECO:0000312|Araport:AT4G18060};
GN ORFNames=F15J5.30 {ECO:0000312|EMBL:CAB53647.1};
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DRP2A.
RX PubMed=12207647; DOI=10.1046/j.1365-313x.2002.01377.x;
RA Lam B.C.-H., Sage T.L., Bianchi F., Blumwald E.;
RT "Regulation of ADL6 activity by its associated molecular network.";
RL Plant J. 31:565-576(2002).
RN [6]
RP INTERACTION WITH FREE1.
RX PubMed=25699591; DOI=10.1104/pp.114.253377;
RA Kolb C., Nagel M.K., Kalinowska K., Hagmann J., Ichikawa M.,
RA Anzenberger F., Alkofer A., Sato M.H., Braun P., Isono E.;
RT "FYVE1 is essential for vacuole biogenesis and intracellular trafficking in
RT Arabidopsis.";
RL Plant Physiol. 167:1361-1373(2015).
RN [7]
RP INTERACTION WITH SH3P2.
RC STRAIN=cv. Columbia, and cv. Wassilewskija-2;
RX PubMed=28584166; DOI=10.1105/tpc.17.00108;
RA Ahn G., Kim H., Kim D.H., Hanh H., Yoon Y., Singaram I., Wijesinghe K.J.,
RA Johnson K.A., Zhuang X., Liang Z., Stahelin R.V., Jiang L., Cho W.,
RA Kang B.-H., Hwang I.;
RT "SH3 domain-containing protein 2 plays a crucial role at the step of
RT membrane tubulation during cell plate formation.";
RL Plant Cell 29:1388-1405(2017).
CC -!- FUNCTION: May be involved in the recruitment of DRP2A to the accessory
CC protein complex and in the negative regulation of its GTPase activity.
CC {ECO:0000305|PubMed:12207647}.
CC -!- SUBUNIT: Interacts with FREE1 (PubMed:25699591). Interacts (via SH3
CC domain) with DRP2A/ADL6 (PubMed:12207647). Binds to SH3P2
CC (PubMed:28584166). {ECO:0000269|PubMed:12207647,
CC ECO:0000269|PubMed:25699591, ECO:0000269|PubMed:28584166}.
CC -!- INTERACTION:
CC Q8L7W0; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-9160890, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:11701884, ECO:0000269|PubMed:12207647}.
CC -!- TISSUE SPECIFICITY: Detected in all tissues except seedlings.
CC {ECO:0000269|PubMed:11701884}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB53647.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78808.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF367775; AAL32440.1; -; mRNA.
DR EMBL; AL110123; CAB53647.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161547; CAB78808.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83989.1; -; Genomic_DNA.
DR EMBL; AY125505; AAM78097.1; -; mRNA.
DR EMBL; BT002255; AAN72266.1; -; mRNA.
DR PIR; T14806; T14806.
DR RefSeq; NP_193540.3; NM_117916.6.
DR AlphaFoldDB; Q8L7W0; -.
DR SMR; Q8L7W0; -.
DR IntAct; Q8L7W0; 9.
DR STRING; 3702.AT4G18060.1; -.
DR PaxDb; Q8L7W0; -.
DR PRIDE; Q8L7W0; -.
DR ProteomicsDB; 234510; -.
DR EnsemblPlants; AT4G18060.1; AT4G18060.1; AT4G18060.
DR GeneID; 827531; -.
DR Gramene; AT4G18060.1; AT4G18060.1; AT4G18060.
DR KEGG; ath:AT4G18060; -.
DR Araport; AT4G18060; -.
DR TAIR; locus:2117666; AT4G18060.
DR eggNOG; ENOG502QZ2M; Eukaryota.
DR HOGENOM; CLU_045749_0_0_1; -.
DR InParanoid; Q8L7W0; -.
DR OMA; QSEAKMI; -.
DR OrthoDB; 788657at2759; -.
DR PhylomeDB; Q8L7W0; -.
DR PRO; PR:Q8L7W0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7W0; baseline and differential.
DR Genevisible; Q8L7W0; AT.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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 Coiled coil; Cytoplasmic vesicle; Reference proteome; SH3 domain.
FT CHAIN 1..351
FT /note="SH3 domain-containing protein 3"
FT /id="PRO_0000434152"
FT DOMAIN 31..267
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 281..340
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT COILED 1..21
FT /evidence="ECO:0000255"
FT COILED 193..213
FT /evidence="ECO:0000255"
FT CONFLICT 99..101
FT /note="NSQ -> IVR (in Ref. 1; AAL32440)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="P -> L (in Ref. 1; AAL32440)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="A -> V (in Ref. 1; AAL32440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39534 MW; A25602ECAD847C45 CRC64;
MDAFRRQASK LRDQVAKQQL AVIKQFSGTG YESSDVMVID ELEMQRHHQL DKLYRSTRSA
KEFQRDIVKA AEAFTTIGLR HIEAGTKLSE DCCRYGNENS QNIDENILAK AAAIYGDARK
HVDKEQEDFN KLLASQVLDP LRAMVAGSPL EDARHLAQRY SRMRQEAETH ATEVSRRQAR
VREAPIPENV AKLQLAEAKM QELKANMAVL GKEATAALAA VESQQHRLTF QRLVAMVEGE
KNYHLRIAAI LSDIEAEMVT EKQHKESAPP AIPTENGSEK TSYFLAEVIH PFSAASEKEL
DLDKGDYIVV RKVSQTGWAE GECKGKAGWF PMAYIEKRQR LPTTNFAAEV Y
