TM1L1_MOUSE
ID TM1L1_MOUSE Reviewed; 474 AA.
AC Q923U0; B0QZV4; Q5SRC7; Q5SRC9; Q99KE0; Q9D6Y5;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=TOM1-like protein 1;
DE AltName: Full=Src-activating and signaling molecule protein;
DE AltName: Full=Target of Myb-like protein 1;
GN Name=Tom1l1; Synonyms=Srcasm;
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 [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION AT
RP TYR-457, AND MUTAGENESIS OF TYR-392; 440-TYR-TYR-441 AND TYR-457.
RC STRAIN=C57BL/6J; TISSUE=Keratinocyte;
RX PubMed=11711534; DOI=10.1074/jbc.m106813200;
RA Seykora J.T., Mei L., Dotto G.P., Stein P.L.;
RT "'Srcasm: a novel Src activating and signaling molecule.";
RL J. Biol. Chem. 277:2812-2822(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Carcinoma;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: Probable adapter protein involved in signaling pathways.
CC Interacts with the SH2 and SH3 domains of various signaling proteins
CC when it is phosphorylated. May promote FYN activation, possibly by
CC disrupting intramolecular SH3-dependent interactions.
CC {ECO:0000269|PubMed:11711534}.
CC -!- SUBUNIT: Interacts with LYN (By similarity). Interacts with the SH2 and
CC SH3 domains of FYN when phosphorylated. Also interacts with GRB2 and
CC PIK3R1 when phosphorylated. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack. Endosome membrane
CC {ECO:0000305}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=A small proportion is membrane-associated.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q923U0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q923U0-2; Sequence=VSP_003996;
CC Name=3;
CC IsoId=Q923U0-3; Sequence=VSP_003997;
CC -!- TISSUE SPECIFICITY: Strongly expressed in brain and kidney, expressed
CC at intermediate levels skin and heart, and weakly expressed in thymus.
CC Not expressed in liver and spleen.
CC -!- PTM: Phosphorylated on tyrosines by LYN (By similarity). Phosphorylated
CC on tyrosines by FYN. {ECO:0000250, ECO:0000269|PubMed:11711534}.
CC -!- SIMILARITY: Belongs to the TOM1 family. {ECO:0000305}.
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DR EMBL; AF395837; AAK83377.1; -; mRNA.
DR EMBL; AK009826; BAB26526.1; -; mRNA.
DR EMBL; AK083630; BAC38972.1; -; mRNA.
DR EMBL; AL672199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004710; AAH04710.1; -; mRNA.
DR CCDS; CCDS88219.1; -. [Q923U0-2]
DR CCDS; CCDS88220.1; -. [Q923U0-3]
DR CCDS; CCDS88221.1; -. [Q923U0-1]
DR RefSeq; XP_006534331.1; XM_006534268.3.
DR AlphaFoldDB; Q923U0; -.
DR SMR; Q923U0; -.
DR BioGRID; 215046; 3.
DR STRING; 10090.ENSMUSP00000103500; -.
DR iPTMnet; Q923U0; -.
DR PhosphoSitePlus; Q923U0; -.
DR MaxQB; Q923U0; -.
DR PaxDb; Q923U0; -.
DR PeptideAtlas; Q923U0; -.
DR PRIDE; Q923U0; -.
DR ProteomicsDB; 259544; -. [Q923U0-1]
DR ProteomicsDB; 259545; -. [Q923U0-2]
DR ProteomicsDB; 259546; -. [Q923U0-3]
DR Antibodypedia; 18249; 256 antibodies from 34 providers.
DR Ensembl; ENSMUST00000020849; ENSMUSP00000020849; ENSMUSG00000020541. [Q923U0-1]
DR Ensembl; ENSMUST00000107867; ENSMUSP00000103499; ENSMUSG00000020541. [Q923U0-2]
DR Ensembl; ENSMUST00000107869; ENSMUSP00000103501; ENSMUSG00000020541. [Q923U0-3]
DR UCSC; uc007kxa.1; mouse. [Q923U0-2]
DR UCSC; uc007kxb.1; mouse. [Q923U0-1]
DR UCSC; uc011ycr.1; mouse. [Q923U0-3]
DR MGI; MGI:1919193; Tom1l1.
DR VEuPathDB; HostDB:ENSMUSG00000020541; -.
DR eggNOG; KOG1087; Eukaryota.
DR GeneTree; ENSGT00940000160240; -.
DR HOGENOM; CLU_1219375_0_0_1; -.
DR InParanoid; Q923U0; -.
DR OMA; HHHKGAQ; -.
DR OrthoDB; 594067at2759; -.
DR PhylomeDB; Q923U0; -.
DR BioGRID-ORCS; 71943; 2 hits in 59 CRISPR screens.
DR ChiTaRS; Tom1l1; mouse.
DR PRO; PR:Q923U0; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q923U0; protein.
DR Bgee; ENSMUSG00000020541; Expressed in seminal vesicle and 231 other tissues.
DR ExpressionAtlas; Q923U0; baseline and differential.
DR Genevisible; Q923U0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0032147; P:activation of protein kinase activity; ISO:MGI.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:MGI.
DR Gene3D; 1.20.58.160; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR004152; GAT_dom.
DR InterPro; IPR038425; GAT_sf.
DR InterPro; IPR014645; TOM1.
DR InterPro; IPR027428; TOM1L1.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR13856:SF28; PTHR13856:SF28; 1.
DR Pfam; PF03127; GAT; 1.
DR Pfam; PF00790; VHS; 1.
DR PIRSF; PIRSF036948; TOM1; 1.
DR SMART; SM00288; VHS; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50909; GAT; 1.
DR PROSITE; PS50179; VHS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endosome; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; SH3-binding;
KW Transport.
FT CHAIN 1..474
FT /note="TOM1-like protein 1"
FT /id="PRO_0000072567"
FT DOMAIN 22..154
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 199..287
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT REGION 153..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..395
FT /note="Interaction with GRB2"
FT REGION 441..444
FT /note="Interaction with PIK3R1"
FT MOTIF 420..424
FT /note="SH3-binding"
FT MOTIF 457..460
FT /note="SH2-binding"
FT COMPBIAS 163..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75674"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75674"
FT MOD_RES 457
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11711534"
FT VAR_SEQ 1..247
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003996"
FT VAR_SEQ 125..200
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_003997"
FT MUTAGEN 392
FT /note="Y->F: Specifically abolishes interaction with GRB2;
FT mild decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:11711534"
FT MUTAGEN 440..441
FT /note="YY->FF: Specifically abolishes interaction with
FT PIK3R1; mild decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:11711534"
FT MUTAGEN 457
FT /note="Y->F: Abolishes phosphorylation by FYN and
FT interaction with FYN."
FT /evidence="ECO:0000269|PubMed:11711534"
FT CONFLICT 414
FT /note="A -> V (in Ref. 2; BAB26526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 52695 MW; 4663AD9C0E6C292C CRC64;
MAFGKSHRDP YATSVGHLIE KATFAGVLTE DWGQFLHICD IINTTQDGPK DAVKALKKRI
SKNYNHKEIQ LSLSLIDMCV QNCGPSFQSL IVKKEFIKDT LVKLLNPRYT LPLETQNRIL
NFIKTWSQGF PGGVDVSEVK EVYLDLLKKG VQFPPSDGEP ETRQEAGQIS PNRPTSVPTA
PALSSIIAPK NPTISLVPEQ IGKLHSELDM VKMNVKVMTA ILMENTPGSE NHEDIELLRK
LYKTGREMQE RIMDLLVVVE NEDVTMELIQ VNEDLNNAVL GYERFTRNQQ RLLEQKRNRT
EATRTSSEPS APSCDLLDLS PIVPVPTPNE GALNSVNAQL SGLSVSSLSP VITNNLYPSL
QPQRDLLASE DIEIPTLFPQ RTSQNLASSH TYDNFHSNSV LLQPVSLHTA TAAAAANQRL
PPLPSSHPVL KDGDLQPPNY YEVMEFDPLA PTTEAVYEEI DGYHQKEAQS HSDC
