STON1_MOUSE
ID STON1_MOUSE Reviewed; 730 AA.
AC Q8CDJ8; Q8CDL8; Q9D5T3;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Stonin-1;
DE AltName: Full=Stoned B-like factor;
GN Name=Ston1; Synonyms=Salf, Sblf, Stn1;
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=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: May be involved in the endocytic machinery. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Note=Some fraction is membrane-associated. {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast to other members of the family, it does not
CC contain NPF (Asn-Pro-Phe) sites and thereby does not interact with
CC EPS15, EPS15R and ITSN1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Stoned B family. {ECO:0000305}.
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DR EMBL; AK014958; BAB29639.1; -; mRNA.
DR EMBL; AK029878; BAC26656.1; -; mRNA.
DR EMBL; AK029959; BAC26699.1; -; mRNA.
DR CCDS; CCDS50207.1; -.
DR RefSeq; NP_084134.2; NM_029858.2.
DR RefSeq; XP_006525174.1; XM_006525111.2.
DR RefSeq; XP_006525175.1; XM_006525112.3.
DR AlphaFoldDB; Q8CDJ8; -.
DR IntAct; Q8CDJ8; 1.
DR STRING; 10090.ENSMUSP00000067027; -.
DR iPTMnet; Q8CDJ8; -.
DR PhosphoSitePlus; Q8CDJ8; -.
DR SwissPalm; Q8CDJ8; -.
DR MaxQB; Q8CDJ8; -.
DR PaxDb; Q8CDJ8; -.
DR PeptideAtlas; Q8CDJ8; -.
DR PRIDE; Q8CDJ8; -.
DR ProteomicsDB; 257497; -.
DR DNASU; 77057; -.
DR Ensembl; ENSMUST00000064035; ENSMUSP00000067027; ENSMUSG00000033855.
DR Ensembl; ENSMUST00000150023; ENSMUSP00000122928; ENSMUSG00000033855.
DR Ensembl; ENSMUST00000163588; ENSMUSP00000131703; ENSMUSG00000033855.
DR GeneID; 77057; -.
DR KEGG; mmu:77057; -.
DR UCSC; uc012ayo.1; mouse.
DR CTD; 11037; -.
DR MGI; MGI:1924307; Ston1.
DR VEuPathDB; HostDB:ENSMUSG00000033855; -.
DR eggNOG; KOG2677; Eukaryota.
DR GeneTree; ENSGT00940000158817; -.
DR HOGENOM; CLU_016541_0_0_1; -.
DR InParanoid; Q8CDJ8; -.
DR OMA; RDGWSVM; -.
DR OrthoDB; 1059322at2759; -.
DR PhylomeDB; Q8CDJ8; -.
DR TreeFam; TF318623; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 77057; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ston1; mouse.
DR PRO; PR:Q8CDJ8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CDJ8; protein.
DR Bgee; ENSMUSG00000033855; Expressed in undifferentiated genital tubercle and 78 other tissues.
DR ExpressionAtlas; Q8CDJ8; baseline and differential.
DR Genevisible; Q8CDJ8; MM.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IDA:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0140312; F:cargo adaptor activity; IDA:MGI.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IDA:MGI.
DR GO; GO:0048041; P:focal adhesion assembly; IMP:MGI.
DR GO; GO:0120181; P:focal adhesion disassembly; IMP:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0030100; P:regulation of endocytosis; ISS:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; IMP:MGI.
DR GO; GO:0006929; P:substrate-dependent cell migration; IMP:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
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; IPR031232; Ston1.
DR InterPro; IPR017110; Stonin.
DR PANTHER; PTHR10529:SF339; PTHR10529:SF339; 1.
DR Pfam; PF00928; Adap_comp_sub; 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; Reference proteome.
FT CHAIN 1..730
FT /note="Stonin-1"
FT /id="PRO_0000185737"
FT DOMAIN 269..402
FT /note="SHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00403"
FT DOMAIN 407..710
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 278
FT /note="E -> V (in Ref. 1; BAC26699)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="C -> F (in Ref. 1; BAC26699)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="E -> D (in Ref. 1; BAB29639)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 730 AA; 81793 MW; FC55399706280B81 CRC64;
MYSTNPGSWV TFDDDPAFQS SQKRKDFSLE TQGVCRPNGL KLTLPTLRDP PSTPSSASST
PLSSPMVDFY FSPGPPSNSP LSTPTKDFPG FPGIPKAGTH VLYPIPECSS SSAPTTAGGV
GPPLLLTKPD CSPHVSLPSS HSHTQPTPTL GFTEDAGPQR VQSEARQFEY FQDHCAFSNP
FWKDEGSASP FPLDSLASRK PFSPKDKEVP IGHKSLTQCS LDYICEKLEH LHSAETQDPL
GDLSMQDPYA GDTVSFVPHS LFRSQPRAGW SFMLRIPEKK NMMSSRQWGP IFLKVLPGGI
LQMYYEKGLE KPFKEFQLDP HCRLSEPKLE NFSMAGKIHT VKVEHVSYSE KRKYHAKTEV
VHEPEVEQML KLGSTEHRDF LEFLTTVEEE LIKLPATAKP KNKSYEEQEI CLDIQDSLWG
KVTKEGQLVE SAVVTQICCL CFLNGPAECF LALNDRELQK RDECYFEKEP EKKGIAILDY
HFHTCVKAEE FEQSRIIKFV PLDACRFELM RFKTSYEAGE LPFAVKSVVT VQGAYVELQA
FVNMTPAAQG SPHAGALRSC NNIMIHFPVP AQWIKALWTR NLQRQKSLKA KMNRRACLGS
LQEPESEPVI QVTVGSAKYE SAYRAVVWKI DRLPDKNSSP DQPHCLSYKL ELGSDQEVPS
DWYPFATVQF SMLEACASRT EVRSLGVESD AQPQKHVCQR ACYNIQVEIE KKWIQVDGED
ADKTGGCVTQ
