KCT2_MOUSE
ID KCT2_MOUSE Reviewed; 259 AA.
AC Q8K201; Q5SVC5; Q922L7; Q9CVN1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Keratinocyte-associated transmembrane protein 2;
DE Flags: Precursor;
GN Name=Kct2;
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 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 [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 34-259.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI24940.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL645589; CAI24940.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC006957; AAH06957.1; -; mRNA.
DR EMBL; BC034829; AAH34829.2; -; mRNA.
DR EMBL; AK007314; BAB24951.1; -; mRNA.
DR CCDS; CCDS24672.1; -.
DR RefSeq; NP_694757.1; NM_153117.2.
DR AlphaFoldDB; Q8K201; -.
DR BioGRID; 229461; 2.
DR STRING; 10090.ENSMUSP00000048441; -.
DR GlyGen; Q8K201; 2 sites.
DR iPTMnet; Q8K201; -.
DR PhosphoSitePlus; Q8K201; -.
DR SwissPalm; Q8K201; -.
DR EPD; Q8K201; -.
DR MaxQB; Q8K201; -.
DR PaxDb; Q8K201; -.
DR PRIDE; Q8K201; -.
DR ProteomicsDB; 269209; -.
DR Antibodypedia; 49872; 70 antibodies from 16 providers.
DR DNASU; 213673; -.
DR Ensembl; ENSMUST00000036952; ENSMUSP00000048441; ENSMUSG00000036275.
DR GeneID; 213673; -.
DR KEGG; mmu:213673; -.
DR UCSC; uc007ivn.1; mouse.
DR MGI; MGI:2654705; 9530068E07Rik.
DR VEuPathDB; HostDB:ENSMUSG00000036275; -.
DR eggNOG; ENOG502S2NF; Eukaryota.
DR GeneTree; ENSGT00440000037499; -.
DR HOGENOM; CLU_091732_0_0_1; -.
DR InParanoid; Q8K201; -.
DR OMA; GEADYDW; -.
DR OrthoDB; 1364680at2759; -.
DR PhylomeDB; Q8K201; -.
DR TreeFam; TF332514; -.
DR BioGRID-ORCS; 213673; 2 hits in 73 CRISPR screens.
DR ChiTaRS; 9530068E07Rik; mouse.
DR PRO; PR:Q8K201; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K201; protein.
DR Bgee; ENSMUSG00000036275; Expressed in stroma of bone marrow and 259 other tissues.
DR ExpressionAtlas; Q8K201; baseline and differential.
DR Genevisible; Q8K201; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR037645; KCT2.
DR PANTHER; PTHR16502; PTHR16502; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..259
FT /note="Keratinocyte-associated transmembrane protein 2"
FT /id="PRO_0000019580"
FT TOPO_DOM 45..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 47..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC54"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC54"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 34
FT /note="V -> R (in Ref. 3; BAB24951)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="N -> Y (in Ref. 3; BAB24951)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28050 MW; 23C9BF719E5BCF3D CRC64;
MAASALGRMC GAAREKLSPG PGARGLGALA RSLVLALLLV PVLCSDRSEN PPNNATVSSP
VVVTAPGNHT SPSVSQISTT LSPASAEKSG SSSAAPTPTA APSAPEEEAD SNEDPSMEEE
DLLALNSSPA TGKDTLDNGD YGEPDYDWTT NPRDEEPEDI NIAISKESRR FRGFQDSVEV
VKLPPPNRED SHFFFHLLIF AFCAAVVYVT YHNKRKIFLL VQSRKWRDGL CSKTVEYHRL
DQNVNEAMPS LKITNDYIF
