STON2_MOUSE
ID STON2_MOUSE Reviewed; 895 AA.
AC Q8BZ60; A2RTJ7;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Stonin-2;
DE AltName: Full=Stoned B;
GN Name=Ston2; Synonyms=Stn2, Stnb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-253 AND SER-759, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Synapse, synaptosome {ECO:0000250}. Note=Some fraction is membrane-
CC associated.
CC -!- DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins
CC involved in the endocytic pathway, mediate the interaction with the EH
CC domain of SYT1, SYT2, EPS15, EPS15R and ITSN1. {ECO:0000250}.
CC -!- PTM: Phosphorylated in vitro by PKD. {ECO:0000250}.
CC -!- PTM: Neddylated; deneddylated via its interaction with the COP9
CC signalosome (CSN) complex through TOR1A and COPS4. {ECO:0000250}.
CC -!- PTM: Ubiquitinated; leading to its degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Stoned B family. {ECO:0000305}.
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DR EMBL; AK036612; BAC29507.1; -; mRNA.
DR EMBL; BC132531; AAI32532.1; -; mRNA.
DR EMBL; BC138054; AAI38055.1; -; mRNA.
DR CCDS; CCDS26090.1; -.
DR RefSeq; NP_780576.1; NM_175367.6.
DR RefSeq; XP_006515436.1; XM_006515373.3.
DR RefSeq; XP_006515437.1; XM_006515374.3.
DR RefSeq; XP_011242284.1; XM_011243982.2.
DR AlphaFoldDB; Q8BZ60; -.
DR SMR; Q8BZ60; -.
DR BioGRID; 224423; 4.
DR IntAct; Q8BZ60; 4.
DR STRING; 10090.ENSMUSP00000053908; -.
DR iPTMnet; Q8BZ60; -.
DR PhosphoSitePlus; Q8BZ60; -.
DR EPD; Q8BZ60; -.
DR MaxQB; Q8BZ60; -.
DR PaxDb; Q8BZ60; -.
DR PRIDE; Q8BZ60; -.
DR ProteomicsDB; 257459; -.
DR ABCD; Q8BZ60; 1 sequenced antibody.
DR Antibodypedia; 164; 29 antibodies from 14 providers.
DR DNASU; 108800; -.
DR Ensembl; ENSMUST00000052969; ENSMUSP00000053908; ENSMUSG00000020961.
DR GeneID; 108800; -.
DR KEGG; mmu:108800; -.
DR UCSC; uc007okt.2; mouse.
DR CTD; 85439; -.
DR MGI; MGI:1918272; Ston2.
DR VEuPathDB; HostDB:ENSMUSG00000020961; -.
DR eggNOG; KOG2677; Eukaryota.
DR GeneTree; ENSGT00940000159392; -.
DR HOGENOM; CLU_016541_0_0_1; -.
DR InParanoid; Q8BZ60; -.
DR OMA; SQPKDGW; -.
DR OrthoDB; 1059322at2759; -.
DR PhylomeDB; Q8BZ60; -.
DR TreeFam; TF300393; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 108800; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ston2; mouse.
DR PRO; PR:Q8BZ60; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BZ60; protein.
DR Bgee; ENSMUSG00000020961; Expressed in animal zygote and 158 other tissues.
DR ExpressionAtlas; Q8BZ60; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IC:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; IDA:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
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_0000185733"
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 15..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..421
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 93..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 278
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:0007744|PubMed:21183079"
SQ SEQUENCE 895 AA; 99611 MW; 2CA089956349B96F CRC64;
MTTLDHVIAT HQSEWVSFSE EPLFPTPLEG GTEEHFPGLS SSSERSESSS GENHVVDEGS
QDLSHSEQDD SSEKMGLISE AASPPGSPVQ PTPDLASAIS NWVQFEDDTP WSSTSPPHKE
TALTLTMPCW TCPSFDSLRR CPLTSESSWT THSEDTSSPS VAPSYTDLQL INTEEQASGR
ASGTDSTDNS SSLQEDEEVE MEAISWWAGS PAMNGHPAAP PVTTARFPSW VTFEDNEVGC
PSPPVPSPKK PNTPSAATAA PDVPFNSTGS FKRDRPKSTL MNLPKVQKLD ISSLNRPPSV
IEAPPWRATN PFLNETLQDV QPSPINPFSA FFEEQERRSQ NSSVSSTTGK SQRDSLIVVY
QDAISFDDSG KSQPHPDAIE KLKQLQIDDP DPVGNTALPD DDPTASVELD APSPASALSQ
PRDGWPMMLR IPEKKNIMSS RHWGPIYIKL TASGYLQLYY EQGLEKPFRE FKLEICHEVS
EPRLQNYDEN GRIHSLRIDR VTYKEKKKYQ PKPAVAHAAE REQVIKLGTT NYDDFRSFIH
AVQDRLMDLP VLSMDLSTVG LNYLEEEITV DVRDEFSGTV GKGDNQILQH HVLTRIHILS
FLSGLAECRL GLNDILIKGN EIVSRQDIMP TTTTKWIKLH ECRFHGCVDE DVFNSSRVIL
FNPLDACRFE LMRFRTVFAE KTLPFTLRTA ASINGAEVEV QSWLRMSPGF SSNRDPLTQV
PCENVMVRYP VPSEWVKNFR RDSVLGEKSL KAKVNRGASF GSAGASGSEP VMRVTLGTAK
YEHAFNSIVW RINRLPDKNS ASGHPHCFFC HLELGSDREV PSRFANYVNV EFSMPTTSAS
KAAVRSVSVE DKPDVRKWVN YSAHYSYKVE IEQKKSLKPD FEGEDLENPK ECGVQ
