STON2_RAT
ID STON2_RAT Reviewed; 895 AA.
AC D4AB66;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Stonin-2;
GN Name=Ston2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP INTERACTION WITH TOR1A AND COPS4, AND SUBCELLULAR LOCATION.
RX PubMed=21102408; DOI=10.1038/emboj.2010.285;
RA Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.;
RT "CSN complex controls the stability of selected synaptic proteins via a
RT torsinA-dependent process.";
RL EMBO J. 30:181-193(2011).
CC -!- FUNCTION: Adapter protein involved in endocytic machinery. Involved in
CC the synaptic vesicle recycling. May facilitate clathrin-coated vesicle
CC uncoating (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the second C2 domain of synaptotagmins SYT1 and
CC SYT2. Interacts with EPS15, EPS15R and ITSN1. Interacts indirectly with
CC the AP-2 adapter complex. Interacts with TOR1A and COPS4; the
CC interaction controls STON2 protein stability.
CC {ECO:0000269|PubMed:21102408}.
CC -!- SUBCELLULAR LOCATION: Synapse, synaptosome
CC {ECO:0000269|PubMed:21102408}. Cytoplasm {ECO:0000250}. Membrane
CC {ECO:0000250}. Note=Some fraction is membrane-associated.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated in vitro by PKD. {ECO:0000250}.
CC -!- PTM: Neddylated and ubiquitinated; leading to its degradation and
CC inhibited by TOR1A and COPS4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Stoned B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR06045586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06045587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06045588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06045589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06045590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06045591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06045592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001129346.1; NM_001135874.1.
DR RefSeq; XP_006240468.1; XM_006240406.3.
DR RefSeq; XP_006240469.1; XM_006240407.3.
DR AlphaFoldDB; D4AB66; -.
DR SMR; D4AB66; -.
DR BioGRID; 260691; 2.
DR IntAct; D4AB66; 3.
DR MINT; D4AB66; -.
DR STRING; 10116.ENSRNOP00000005881; -.
DR iPTMnet; D4AB66; -.
DR PhosphoSitePlus; D4AB66; -.
DR PaxDb; D4AB66; -.
DR PeptideAtlas; D4AB66; -.
DR PRIDE; D4AB66; -.
DR ABCD; D4AB66; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000005881; ENSRNOP00000005881; ENSRNOG00000004458.
DR GeneID; 314349; -.
DR KEGG; rno:314349; -.
DR UCSC; RGD:1311502; rat.
DR CTD; 85439; -.
DR RGD; 1311502; Ston2.
DR eggNOG; KOG2677; Eukaryota.
DR GeneTree; ENSGT00940000159392; -.
DR HOGENOM; CLU_016541_0_0_1; -.
DR InParanoid; D4AB66; -.
DR OMA; SQPKDGW; -.
DR OrthoDB; 1059322at2759; -.
DR PhylomeDB; D4AB66; -.
DR TreeFam; TF300393; -.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:D4AB66; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004458; Expressed in frontal cortex and 16 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR012320; SHD_dom.
DR InterPro; IPR031228; STON2.
DR InterPro; IPR017110; Stonin.
DR InterPro; IPR022699; Stonin2_N.
DR PANTHER; PTHR10529:SF345; PTHR10529:SF345; 1.
DR Pfam; PF00928; Adap_comp_sub; 1.
DR Pfam; PF12016; Stonin2_N; 1.
DR PIRSF; PIRSF037099; Stonin; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR PROSITE; PS51072; MHD; 1.
DR PROSITE; PS51070; SHD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endocytosis; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; Synaptosome; Ubl conjugation.
FT CHAIN 1..895
FT /note="Stonin-2"
FT /id="PRO_0000429277"
FT DOMAIN 424..557
FT /note="SHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00403"
FT DOMAIN 565..872
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 10..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 310..312
FT /note="NPF 1"
FT MOTIF 326..328
FT /note="NPF 2"
FT COMPBIAS 36..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE9"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE9"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE9"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXE9"
SQ SEQUENCE 895 AA; 99491 MW; 692E1308E897F35C CRC64;
MTTLDHVIAT HQSEWVSFSE EPLFPTPLEG GTEEHFPGLS SSSDRSESSS GENHAVDEGS
QDLSHSEQDD SSEKMGLISE AASPPGSPVQ PTPDLASAIS NWVQFEDDTP WSNTSAPHKE
TALTLTVPCW TCPSLDSLRR CPLASESSWT THSEDTSSPS VAPSYTDLQL INAEEQASGR
ASGTDSTDNS SSLQEDEEVE METISWWAGS PAMNGHPAVP QVTTARFPSW VTFEDNEVGC
PSPTVPSPKK PNAPSAATAG PDVPFNSTGS FKRDRPKSTL MNLSKVQKLD ISSLNRPPSV
TEAPPWRATN PFLNESLQDI QPSPINPFSA FFEEQERRSQ NSSISGTSGK SQRDSLIVIY
QDAISFDDSG KSQSHPDAIE KLKQLQIDDP DPVGNAALPD DDPTASVEPD APSPTSALSQ
PRDGWPMMLR IPEKKNIMSS RHWGPIYIKL TDSGYLQLYY EQGLEKPFRE FKLEICHEVS
EPRLQNYDEN GRIHSLRIDR VTYKEKKKYQ PKPAVAHAAE REQVIKLGTT NYDDFLSFIH
AVQDRLMDLP VQSMDLSTVG LNYLEEEITV DIRDEFSGTV SKGDNQILQH HVLTRIHILS
FLSGLAECRL GLNDILIKGN EIVSRQDIMP TTTTKWIKLH ECRFHGCVDE DVFNSSRVIL
FNPLDACRFE LMRFRTVFAE KTLPFTLRTA ASINGAEVEV QSWLRMSPGF SSNRDPLTQV
PCENVMVRYP VPSEWVKNFR RESVLGEKSL KAKVNRGASF GSAGASGSEP VMRVTLGTAK
YEHAFNSIVW RINRLPDKNS ASGHPHCFFC HLELGSDREV PSRFANHVNV EFSMPTTSAS
KAAVRSISVE DKPDVRKWVN YSAHYSYKVE IEQKKSLKPD FEGEDLENPK ECGVQ
