TM1L1_RAT
ID TM1L1_RAT Reviewed; 475 AA.
AC F1LM81;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 25-MAY-2022, entry version 63.
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 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 LYN, SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY LYN.
RX PubMed=17977829; DOI=10.1074/jbc.m705168200;
RA Zhang J., Suzuki K., Hitomi T., Siraganian R.P.;
RT "TOM1L1 is a Lyn substrate involved in FcepsilonRI signaling in mast
RT cells.";
RL J. Biol. Chem. 282:37669-37677(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the SH2 and SH3 domains of FYN when
CC phosphorylated. Also interacts with GRB2 and PIK3R1 when phosphorylated
CC (By similarity). Interacts with LYN. {ECO:0000250,
CC ECO:0000269|PubMed:17977829}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack {ECO:0000250}.
CC Endosome membrane {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:17977829}. Membrane {ECO:0000269|PubMed:17977829};
CC Peripheral membrane protein {ECO:0000269|PubMed:17977829}; Cytoplasmic
CC side {ECO:0000269|PubMed:17977829}. Note=A small proportion is
CC membrane-associated.
CC -!- PTM: Phosphorylated on tyrosines by FYN and LYN.
CC {ECO:0000269|PubMed:17977829}.
CC -!- SIMILARITY: Belongs to the TOM1 family. {ECO:0000305}.
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DR EMBL; AABR03074187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03074211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03076121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03076904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1LM81; -.
DR SMR; F1LM81; -.
DR STRING; 10116.ENSRNOP00000003369; -.
DR iPTMnet; F1LM81; -.
DR PhosphoSitePlus; F1LM81; -.
DR jPOST; F1LM81; -.
DR PaxDb; F1LM81; -.
DR PRIDE; F1LM81; -.
DR RGD; 1562626; Tom1l1.
DR eggNOG; KOG1087; Eukaryota.
DR HOGENOM; CLU_043812_0_0_1; -.
DR InParanoid; F1LM81; -.
DR TreeFam; TF314105; -.
DR PRO; PR:F1LM81; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; F1LM81; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
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:RGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
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:RGD.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; ISO:RGD.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
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 Cytoplasm; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; SH3-binding; Transport.
FT CHAIN 1..475
FT /note="TOM1-like protein 1"
FT /id="PRO_0000414590"
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 155..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..395
FT /note="Interaction with GRB2"
FT /evidence="ECO:0000250"
FT REGION 442..445
FT /note="Interaction with PIK3R1"
FT /evidence="ECO:0000250"
FT MOTIF 421..425
FT /note="SH3-binding"
FT /evidence="ECO:0000250"
FT MOTIF 458..461
FT /note="SH2-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 296..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923U0"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75674"
FT MOD_RES 458
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q923U0"
SQ SEQUENCE 475 AA; 52551 MW; F1071ECB70D862F2 CRC64;
MAFGKSHRDP YATSLGHLIE KATFAGVQTE DWGQFMHICD IINTTQDGPK DAVKALKKRI
SKNYNHKEIQ LSLSLIDMCM QNCGPSFQSL IVKKEFVKDT LVKLLNPRYT LPLETQNRIL
SFIKMWSQGF PGGVDVSEVK EVYLDLLKKG VQFPPLDGEP ETKQEAGQIS PSRPTSVPTA
PALSSIIAPK NPTISLVPEQ IGKLHSELDM VKMNVKVMTA ILMENTPGSE NHEDIELLRK
LYKTGREMQE RIMDLLVVVE NEDVTVELIQ VNEDLNNAIL GYERFTRNQQ RLLEQKRNPT
EANQTSSEPS APSCDLLNLG PVAPVPVSSE GPLNSVNAQL SGLNVSSQSP VITNNLYPSL
QPQMDLLASE DTEVPTLFPQ RTSQNLASSH TYDNFPDHSS SVLLQPVSLH TAPAAPSSQR
LPPLPSNHPV LKNSALQPPS YYEVMEFDPL APTTEAIYEE IDASHKKGAQ SHSEC
