TMM40_MOUSE
ID TMM40_MOUSE Reviewed; 225 AA.
AC Q4FJU9; Q8C5D2; Q8VCR5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Transmembrane protein 40;
GN Name=Tmem40;
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].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-225.
RC STRAIN=C57BL/6J; TISSUE=Colon;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37427.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CT010303; CAJ18511.1; -; mRNA.
DR EMBL; BC019416; AAH19416.1; -; mRNA.
DR EMBL; AK078864; BAC37427.1; ALT_INIT; mRNA.
DR CCDS; CCDS39601.1; -.
DR RefSeq; NP_001161728.1; NM_001168256.1.
DR RefSeq; NP_659054.2; NM_144805.2.
DR RefSeq; XP_006506882.1; XM_006506819.3.
DR RefSeq; XP_011239813.1; XM_011241511.2.
DR RefSeq; XP_017177335.1; XM_017321846.1.
DR AlphaFoldDB; Q4FJU9; -.
DR STRING; 10090.ENSMUSP00000108568; -.
DR iPTMnet; Q4FJU9; -.
DR PhosphoSitePlus; Q4FJU9; -.
DR MaxQB; Q4FJU9; -.
DR PaxDb; Q4FJU9; -.
DR PRIDE; Q4FJU9; -.
DR ProteomicsDB; 259429; -.
DR Antibodypedia; 26279; 40 antibodies from 10 providers.
DR DNASU; 94346; -.
DR Ensembl; ENSMUST00000072933; ENSMUSP00000072704; ENSMUSG00000059900.
DR Ensembl; ENSMUST00000166254; ENSMUSP00000131697; ENSMUSG00000059900.
DR GeneID; 94346; -.
DR KEGG; mmu:94346; -.
DR UCSC; uc009dja.3; mouse.
DR CTD; 55287; -.
DR MGI; MGI:2137870; Tmem40.
DR VEuPathDB; HostDB:ENSMUSG00000059900; -.
DR eggNOG; ENOG502SRH1; Eukaryota.
DR GeneTree; ENSGT00390000017530; -.
DR InParanoid; Q4FJU9; -.
DR OMA; NDEDQHP; -.
DR PhylomeDB; Q4FJU9; -.
DR BioGRID-ORCS; 94346; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Tmem40; mouse.
DR PRO; PR:Q4FJU9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q4FJU9; protein.
DR Bgee; ENSMUSG00000059900; Expressed in epithelium of lens and 152 other tissues.
DR ExpressionAtlas; Q4FJU9; baseline and differential.
DR Genevisible; Q4FJU9; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR026181; TMEM40.
DR PANTHER; PTHR16108; PTHR16108; 1.
DR Pfam; PF15817; TMEM40; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..225
FT /note="Transmembrane protein 40"
FT /id="PRO_0000280359"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWA1"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 130
FT /note="G -> C (in Ref. 3; BAC37427)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="F -> S (in Ref. 2; AAH19416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 24926 MW; FEDE7FB6298FC22B CRC64;
MEASGSSSQS QDSGGVHRET EDHYQETELH KHHGKARERY KRDKSSSSSS SSSSSSSSSS
SSSSSSSDSS DEDQPSRGPR KHRRRPRRDS LRGADHGELE VLKDELQLCG GAAGEMVPTG
ESGLRRRGSG SAEGEVEASQ LRRLNIKKDD EFFHFVLLCF AIGALLVCYH YYADWFMSLG
VGLLTFASLE TIGIYFGLVY RIHSVLQGFI PLLQKFRLPG FRRTN
