TM1L2_MOUSE
ID TM1L2_MOUSE Reviewed; 507 AA.
AC Q5SRX1; A0JP66; Q5SRX7; Q5SRY0; Q6P5D7; Q8C6J0; Q8C935; Q8CB51; Q8R4H1;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=TOM1-like protein 2;
DE AltName: Full=Target of Myb-like protein 2;
GN Name=Tom1l2;
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), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11997338; DOI=10.1101/gr.73702;
RA Bi W., Yan J., Stankiewicz P., Park S.-S., Walz K., Boerkoel C.F.,
RA Potocki L., Shaffer L.G., Devriendt K., Nowaczyk M.J.M., Inoue K.,
RA Lupski J.R.;
RT "Genes in a refined Smith-Magenis syndrome critical deletion interval on
RT chromosome 17p11.2 and the syntenic region of the mouse.";
RL Genome Res. 12:713-728(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Lung, Ovary, and Vagina;
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 STRAIN=C57BL/6J; 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
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 role in protein transport. May regulate growth
CC factor-induced mitogenic signaling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with clathrin, SRC and TOLLIP. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5SRX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SRX1-2; Sequence=VSP_023396;
CC Name=3;
CC IsoId=Q5SRX1-3; Sequence=VSP_023397, VSP_023398;
CC Name=4;
CC IsoId=Q5SRX1-4; Sequence=VSP_023395, VSP_023399;
CC Name=5;
CC IsoId=Q5SRX1-5; Sequence=VSP_023393, VSP_023394;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Splicing pattern displays
CC tissue specific variation. {ECO:0000269|PubMed:11997338}.
CC -!- DOMAIN: The GAT domain mediates interaction with TOLLIP. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TOM1 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; AF467887; AAL77033.1; -; mRNA.
DR EMBL; AK036788; BAC29576.1; -; mRNA.
DR EMBL; AK043095; BAC31458.1; -; mRNA.
DR EMBL; AK054531; BAC35813.1; -; mRNA.
DR EMBL; AK166040; BAE38537.1; -; mRNA.
DR EMBL; AL596090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC062947; AAH62947.2; -; mRNA.
DR EMBL; BC127266; AAI27267.1; -; mRNA.
DR CCDS; CCDS24786.1; -. [Q5SRX1-1]
DR CCDS; CCDS24787.1; -. [Q5SRX1-3]
DR CCDS; CCDS36171.1; -. [Q5SRX1-2]
DR CCDS; CCDS88165.1; -. [Q5SRX1-4]
DR RefSeq; NP_001034181.1; NM_001039092.3. [Q5SRX1-2]
DR RefSeq; NP_001034182.1; NM_001039093.1. [Q5SRX1-3]
DR RefSeq; NP_694720.2; NM_153080.2. [Q5SRX1-1]
DR RefSeq; XP_006532930.1; XM_006532867.3.
DR AlphaFoldDB; Q5SRX1; -.
DR SMR; Q5SRX1; -.
DR BioGRID; 229791; 6.
DR IntAct; Q5SRX1; 1.
DR MINT; Q5SRX1; -.
DR STRING; 10090.ENSMUSP00000099744; -.
DR iPTMnet; Q5SRX1; -.
DR PhosphoSitePlus; Q5SRX1; -.
DR EPD; Q5SRX1; -.
DR jPOST; Q5SRX1; -.
DR MaxQB; Q5SRX1; -.
DR PaxDb; Q5SRX1; -.
DR PeptideAtlas; Q5SRX1; -.
DR PRIDE; Q5SRX1; -.
DR ProteomicsDB; 258906; -. [Q5SRX1-1]
DR ProteomicsDB; 258907; -. [Q5SRX1-2]
DR ProteomicsDB; 258908; -. [Q5SRX1-3]
DR ProteomicsDB; 258909; -. [Q5SRX1-4]
DR ProteomicsDB; 258910; -. [Q5SRX1-5]
DR Antibodypedia; 13414; 148 antibodies from 25 providers.
DR DNASU; 216810; -.
DR Ensembl; ENSMUST00000064019; ENSMUSP00000063414; ENSMUSG00000000538. [Q5SRX1-4]
DR Ensembl; ENSMUST00000095254; ENSMUSP00000092884; ENSMUSG00000000538. [Q5SRX1-2]
DR Ensembl; ENSMUST00000102682; ENSMUSP00000099743; ENSMUSG00000000538. [Q5SRX1-3]
DR Ensembl; ENSMUST00000102683; ENSMUSP00000099744; ENSMUSG00000000538. [Q5SRX1-1]
DR GeneID; 216810; -.
DR KEGG; mmu:216810; -.
DR UCSC; uc007jfq.1; mouse. [Q5SRX1-1]
DR UCSC; uc007jfr.1; mouse. [Q5SRX1-2]
DR UCSC; uc007jft.1; mouse. [Q5SRX1-3]
DR CTD; 146691; -.
DR MGI; MGI:2443306; Tom1l2.
DR VEuPathDB; HostDB:ENSMUSG00000000538; -.
DR eggNOG; KOG1087; Eukaryota.
DR GeneTree; ENSGT00940000156940; -.
DR HOGENOM; CLU_043812_3_0_1; -.
DR InParanoid; Q5SRX1; -.
DR OMA; QKWINDA; -.
DR OrthoDB; 1213216at2759; -.
DR PhylomeDB; Q5SRX1; -.
DR TreeFam; TF314105; -.
DR BioGRID-ORCS; 216810; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tom1l2; mouse.
DR PRO; PR:Q5SRX1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SRX1; protein.
DR Bgee; ENSMUSG00000000538; Expressed in habenula and 211 other tissues.
DR ExpressionAtlas; Q5SRX1; baseline and differential.
DR Genevisible; Q5SRX1; MM.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
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:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; ISO: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; IPR027429; TOM1L2.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR13856:SF31; PTHR13856:SF31; 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; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..507
FT /note="TOM1-like protein 2"
FT /id="PRO_0000278791"
FT DOMAIN 20..152
FT /note="VHS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00218"
FT DOMAIN 219..307
FT /note="GAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00373"
FT REGION 164..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 329..334
FT /note="Clathrin-binding"
FT COMPBIAS 177..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZVM7"
FT VAR_SEQ 260..286
FT /note="ELNRTCRAMQHRIVELISRVSNEEVTE -> VFQVCPSTAHESNRETCELLV
FT WRFLEK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023393"
FT VAR_SEQ 287..507
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023394"
FT VAR_SEQ 427..450
FT /note="IPVAQPSVMDDIEVWLRTDLKGDD -> EMYGNACLSAWQGRRRLPGPPGLE
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023395"
FT VAR_SEQ 427..446
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023396"
FT VAR_SEQ 427..440
FT /note="IPVAQPSVMDDIEV -> VGLHTCVLPTVFWR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023397"
FT VAR_SEQ 441..507
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023398"
FT VAR_SEQ 451..507
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023399"
FT CONFLICT 42
FT /note="E -> K (in Ref. 4; AAH62947)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="S -> G (in Ref. 2; BAC29576)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="A -> T (in Ref. 1; AAL77033)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="D -> G (in Ref. 2; BAC31458)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 55663 MW; BE1A56C6EFEE7F25 CRC64;
MEFLLGNPFS TPVGQCLEKA TDGSLQSEDW TLNMEICDII NETEEGPKDA IRALKKRLSG
NRNYREVMLA LTVLETCVKN CGHRFHLLVA NRDFIDSVLV KIISPKNNPP TIVQDKVLAL
IQAWADAFRS SPDLTGVVHI YEELKRRGIE FPMADLDALS PIHTPQRSVP EMDPAATIPR
SQTQPRTTAG TYSSPPPASY STLQAPALSV TGPITANSEQ IARLRSELDI VRGNTKVMSE
MLTEMVPGQE DSSDLELLQE LNRTCRAMQH RIVELISRVS NEEVTEELLH VNDDLNNVFL
RYERFERYRS GRSVQNASNG VLSEVTEDNL IDLGPGSPAV VSPMVGSTAP PSSLSSQLAG
LDLGTESVSG TLSSLQQCKP QDGFDMFAQT RGNSLAEQRK TVTYEDPQAV GGLASALDNR
KQNSEMIPVA QPSVMDDIEV WLRTDLKGDD LEEGVTSEEF DKFLEERAKA AETVPDLPSP
PTEAPAPASN TSTRKKPERS DDALFAL
