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SH3 domain-containing protein 2

 SH3P2_ARATH             Reviewed;         368 AA.
Q8VWF1; F4JLF5; F4JLF6; O65689;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
16-JAN-2019, entry version 122.
RecName: Full=SH3 domain-containing protein 2 {ECO:0000312|EMBL:AAL32439.1};
Name=SH3P2;
OrderedLocusNames=At4g34660 {ECO:0000312|Araport:AT4G34660};
ORFNames=T4L20.240 {ECO:0000312|EMBL:CAA18845.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|EMBL:AAL59954.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=11701884; DOI=10.1105/tpc.13.11.2499;
Lam B.C.-H., Sage T.L., Bianchi F., Blumwald E.;
"Role of SH3 domain-containing proteins in clathrin-mediated vesicle
trafficking in Arabidopsis.";
Plant Cell 13:2499-2512(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
SUBCELLULAR LOCATION, AND INTERACTION WITH FREE1.
PubMed=25699591; DOI=10.1104/pp.114.253377;
Kolb C., Nagel M.K., Kalinowska K., Hagmann J., Ichikawa M.,
Anzenberger F., Alkofer A., Sato M.H., Braun P., Isono E.;
"FYVE1 is essential for vacuole biogenesis and intracellular
trafficking in Arabidopsis.";
Plant Physiol. 167:1361-1373(2015).
[7]
INTERACTION WITH FREE1, DOMAIN, AND IDENTIFICATION IN A PI3K COMPLEX.
PubMed=25624505; DOI=10.1073/pnas.1421271112;
Gao C., Zhuang X., Cui Y., Fu X., He Y., Zhao Q., Zeng Y., Shen J.,
Luo M., Jiang L.;
"Dual roles of an Arabidopsis ESCRT component FREE1 in regulating
vacuolar protein transport and autophagic degradation.";
Proc. Natl. Acad. Sci. U.S.A. 112:1886-1891(2015).
[8]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH ATG8E AND
ATG8F, AND IDENTIFICATION IN A PI3K COMPLEX.
PubMed=24249832; DOI=10.1105/tpc.113.118307;
Zhuang X., Wang H., Lam S.K., Gao C., Wang X., Cai Y., Jiang L.;
"A BAR-domain protein SH3P2, which binds to phosphatidylinositol 3-
phosphate and ATG8, regulates autophagosome formation in
Arabidopsis.";
Plant Cell 25:4596-4615(2013).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.4161/auto.28060;
Zhuang X., Jiang L.;
"Autophagosome biogenesis in plants.";
Autophagy 10:704-705(2014).
-!- FUNCTION: Regulator for autophaosome formation and/or maturation
(PubMed:24249832, Ref.9). Binds phosphatidylinositol 3-phosphate
(PubMed:24249832). {ECO:0000269|PubMed:24249832,
ECO:0000269|Ref.9}.
-!- SUBUNIT: Homodimer (PubMed:24249832). Interacts with FREE1
(PubMed:25699591, PubMed:25624505). Interacts (via SH3 domain)
with ATG8E and ATG8F (PubMed:24249832). Component of a
phosphoinositide 3-kinase (PI3K) complex containing ATG6, SH3P2
and FREE1 (PubMed:25624505, PubMed:24249832).
{ECO:0000269|PubMed:24249832, ECO:0000269|PubMed:25624505,
ECO:0000269|PubMed:25699591}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24249832,
ECO:0000269|PubMed:25699591}. Cytoplasmic vesicle, clathrin-coated
vesicle {ECO:0000269|PubMed:11701884,
ECO:0000269|PubMed:25699591}. Cell membrane
{ECO:0000269|PubMed:25699591}. Late endosome
{ECO:0000269|PubMed:25699591}. Cytoplasmic vesicle, autophagosome
membrane {ECO:0000269|PubMed:24249832, ECO:0000269|Ref.9};
Peripheral membrane protein {ECO:0000269|Ref.9}. Note=Transolcate
from the cytosol to the phagophore assembly site/preautophagosome
structure upon autophagy induction. {ECO:0000269|PubMed:24249832}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8VWF1-1; Sequence=Displayed;
Name=2;
IsoId=Q8VWF1-2; Sequence=VSP_057911;
Name=3;
IsoId=Q8VWF1-3; Sequence=VSP_057912;
-!- TISSUE SPECIFICITY: Highly expressed in seedlings. Detected in
flowers, leaves and stems. {ECO:0000269|PubMed:11701884}.
-!- DOMAIN: The N-terminal BAR domain is required for the interaction
with FREE1. {ECO:0000269|PubMed:25624505}.
-!- MISCELLANEOUS: Knockdown of SH3P2 is developmentally lethal and
significantly suppresses autophagosome formation.
{ECO:0000269|PubMed:24249832}.
-!- SEQUENCE CAUTION:
Sequence=CAA18845.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB80183.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF367774; AAL32439.1; -; mRNA.
EMBL; AL023094; CAA18845.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161585; CAB80183.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE86405.1; -; Genomic_DNA.
EMBL; CP002687; AEE86406.1; -; Genomic_DNA.
EMBL; CP002687; AEE86407.1; -; Genomic_DNA.
EMBL; AY072132; AAL59954.1; -; mRNA.
EMBL; AY096478; AAM20118.1; -; mRNA.
EMBL; AY087158; AAM64716.1; -; mRNA.
PIR; T05286; T05286.
RefSeq; NP_001190913.1; NM_001203984.1. [Q8VWF1-2]
RefSeq; NP_001190914.1; NM_001203985.1. [Q8VWF1-3]
RefSeq; NP_567969.1; NM_119632.4. [Q8VWF1-1]
UniGene; At.2311; -.
ProteinModelPortal; Q8VWF1; -.
SMR; Q8VWF1; -.
IntAct; Q8VWF1; 2.
STRING; 3702.AT4G34660.1; -.
iPTMnet; Q8VWF1; -.
PaxDb; Q8VWF1; -.
PRIDE; Q8VWF1; -.
EnsemblPlants; AT4G34660.1; AT4G34660.1; AT4G34660. [Q8VWF1-1]
EnsemblPlants; AT4G34660.2; AT4G34660.2; AT4G34660. [Q8VWF1-2]
EnsemblPlants; AT4G34660.3; AT4G34660.3; AT4G34660. [Q8VWF1-3]
GeneID; 829618; -.
Gramene; AT4G34660.1; AT4G34660.1; AT4G34660. [Q8VWF1-1]
Gramene; AT4G34660.2; AT4G34660.2; AT4G34660. [Q8VWF1-2]
Gramene; AT4G34660.3; AT4G34660.3; AT4G34660. [Q8VWF1-3]
KEGG; ath:AT4G34660; -.
Araport; AT4G34660; -.
TAIR; locus:2139554; AT4G34660.
eggNOG; ENOG410IIP7; Eukaryota.
eggNOG; ENOG4110148; LUCA.
HOGENOM; HOG000242335; -.
InParanoid; Q8VWF1; -.
OMA; MAYKLEA; -.
OrthoDB; 788657at2759; -.
PhylomeDB; Q8VWF1; -.
PRO; PR:Q8VWF1; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q8VWF1; baseline and differential.
Genevisible; Q8VWF1; AT.
GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0009504; C:cell plate; IDA:TAIR.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0043130; F:ubiquitin binding; IDA:TAIR.
GO; GO:0009920; P:cell plate formation involved in plant-type cell wall biogenesis; IDA:TAIR.
GO; GO:0072583; P:clathrin-dependent endocytosis; IPI:TAIR.
Gene3D; 1.20.1270.60; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF14604; SH3_9; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF103657; SSF103657; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Coiled coil; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Endosome; Membrane;
Reference proteome; SH3 domain.
CHAIN 1 368 SH3 domain-containing protein 2.
/FTId=PRO_0000434151.
DOMAIN 1 264 BAR. {ECO:0000255|PROSITE-
ProRule:PRU00361}.
DOMAIN 299 358 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COMPBIAS 27 34 Poly-Gly. {ECO:0000255}.
COMPBIAS 275 278 Poly-Pro. {ECO:0000255}.
VAR_SEQ 20 42 Missing (in isoform 2).
/FTId=VSP_057911.
VAR_SEQ 253 303 Missing (in isoform 3).
/FTId=VSP_057912.
SEQUENCE 368 AA; 40925 MW; FBC1EB62BCEEE9D8 CRC64;
MDAIRKQASR LREQVARQQQ AVFKQFGGGG YGSGLADEAE LNQHQKLEKL YISTRAAKHY
QRDIVRGVEG YIVTGSKQVE IGTKLSEDSR KYGSENTCTN GNVLTRAALN YGRARAQMEK
ERGNMLKALG TQVAEPLRAM VLGAPLEDAR HLAQRYDRMR QEAEAQATEV ARRQAKARES
QGNPDILMKL ESAEAKLHDL KSNMTILGKE AASALASVED QQQKLTLERL LSMVESERAY
HQRVLQILDQ LEGEMVSERQ RIEAPSTPSS ADSMPPPPSY EEANGVFASQ MHDTSTDSMG
YFLGEVLFPY HGVTDVELSL STGEYVVVRK VTGSGWAEGE CKGKAGWFPY GYIERRERVL
ASKVSEVF


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