ID KT33A_MOUSE Reviewed; 404 AA. AC Q8K0Y2; Q9D7C4; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 24-JAN-2024, entry version 154. DE RecName: Full=Keratin, type I cuticular Ha3-I {ECO:0000250|UniProtKB:O76009}; DE AltName: Full=Hair keratin, type I Ha3-I; DE AltName: Full=Keratin-33A {ECO:0000250|UniProtKB:O76009, ECO:0000312|EMBL:AAH29257.1}; DE Short=K33A; GN Name=Krt33a {ECO:0000312|MGI:MGI:1919138}; 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] {ECO:0000312|EMBL:BAC29777.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29777.1}; RC TISSUE=Neonatal skin {ECO:0000312|EMBL:BAC29777.1}, and Tongue RC {ECO:0000312|EMBL:BAB26243.1}; 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 [2] 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 [3] {ECO:0000312|EMBL:CAM22478.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000312|EMBL:AAH29257.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH29257.1}; RC TISSUE=Salivary gland {ECO:0000312|EMBL:AAH29257.1}; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; 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 -!- MISCELLANEOUS: There are two types of hair/microfibrillar keratin, I CC (acidic) and II (neutral to basic). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. 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; AK009363; BAB26243.1; -; mRNA. DR EMBL; AK037251; BAC29777.1; -; mRNA. DR EMBL; AL592545; CAM22478.1; -; Genomic_DNA. DR EMBL; CH466662; EDL02593.1; -; Genomic_DNA. DR EMBL; BC029257; AAH29257.1; -; mRNA. DR CCDS; CCDS25403.1; -. DR RefSeq; NP_082259.2; NM_027983.3. DR AlphaFoldDB; Q8K0Y2; -. DR SMR; Q8K0Y2; -. DR BioGRID; 215008; 1. DR IntAct; Q8K0Y2; 1. DR MINT; Q8K0Y2; -. DR STRING; 10090.ENSMUSP00000018399; -. DR PhosphoSitePlus; Q8K0Y2; -. DR EPD; Q8K0Y2; -. DR jPOST; Q8K0Y2; -. DR PaxDb; 10090-ENSMUSP00000018399; -. DR PeptideAtlas; Q8K0Y2; -. DR ProteomicsDB; 264880; -. DR DNASU; 71888; -. DR Ensembl; ENSMUST00000018399.3; ENSMUSP00000018399.3; ENSMUSG00000035592.3. DR GeneID; 71888; -. DR KEGG; mmu:71888; -. DR UCSC; uc007lka.2; mouse. DR AGR; MGI:1919138; -. DR CTD; 3883; -. DR MGI; MGI:1919138; Krt33a. DR VEuPathDB; HostDB:ENSMUSG00000035592; -. DR eggNOG; ENOG502SNBF; Eukaryota. DR GeneTree; ENSGT00940000153980; -. DR HOGENOM; CLU_012560_8_0_1; -. DR InParanoid; Q8K0Y2; -. DR OMA; ACNISAN; -. DR OrthoDB; 4640531at2759; -. DR PhylomeDB; Q8K0Y2; -. DR TreeFam; TF332742; -. DR Reactome; R-MMU-6805567; Keratinization. DR Reactome; R-MMU-6809371; Formation of the cornified envelope. DR BioGRID-ORCS; 71888; 4 hits in 76 CRISPR screens. DR PRO; PR:Q8K0Y2; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q8K0Y2; Protein. DR Bgee; ENSMUSG00000035592; Expressed in lip and 15 other cell types or tissues. DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central. DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central. DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR002957; Keratin_I. DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1. DR PANTHER; PTHR23239:SF97; KERATIN, TYPE I CUTICULAR HA1; 1. DR Pfam; PF00038; Filament; 1. DR PRINTS; PR01248; TYPE1KERATIN. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR Genevisible; Q8K0Y2; MM. PE 1: Evidence at protein level; KW Coiled coil; Intermediate filament; Keratin; Reference proteome. FT CHAIN 1..404 FT /note="Keratin, type I cuticular Ha3-I" FT /id="PRO_0000366205" FT DOMAIN 56..367 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..56 FT /note="Head" FT /evidence="ECO:0000255" FT REGION 57..91 FT /note="Coil 1A" FT /evidence="ECO:0000255" FT REGION 92..102 FT /note="Linker 1" FT /evidence="ECO:0000255" FT REGION 103..203 FT /note="Coil 1B" FT /evidence="ECO:0000255" FT REGION 204..219 FT /note="Linker 12" FT /evidence="ECO:0000255" FT REGION 220..363 FT /note="Coil 2" FT /evidence="ECO:0000255" FT REGION 364..404 FT /note="Tail" FT /evidence="ECO:0000255" FT SITE 305 FT /note="Stutter" FT /evidence="ECO:0000255" FT CONFLICT 240 FT /note="R -> L (in Ref. 1; BAB26243)" FT /evidence="ECO:0000305" SQ SEQUENCE 404 AA; 46137 MW; 15C54491027291DF CRC64; MPYNCCLPAM SCRTSCSSRP CVPPSCHGCT LPGACNIPAN VGNCNWFCEG SFNGNEKETM QFLNDRLASY MEKVRQLERE NAELECRIQE RNQQQDPLVC PAYQAYFRTI EELQQKILCG KSENARLVVQ IDNAKLASDD FRTKYETELS LRQLVEADIN SLRRILDELT LCKSDLEAQV ESLKEELLCL KQNHEQEVNT LRCQLGDRLN VEVDAAPTVD LNRVLNETRC QYEALVETNR REVEEWYTTQ TEELNKQVVS SSEQLQSCQA EIIELRRTVN ALEIELQAQH ELRNSLENTL TESEARYSSQ LSQVQCLITN VESQLGEIRA DLERQNQEYQ VLLDIRSRLE CEINTYRGLL ESEDCKLPCN PCATTNACDK PIGPCVPNPC VTRPRCGPCN TFVR //