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Database: UniProt
Entry: KRT34_MOUSE
LinkDB: KRT34_MOUSE
Original site: KRT34_MOUSE 
ID   KRT34_MOUSE             Reviewed;         392 AA.
AC   Q9D646;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Keratin, type I cuticular Ha4 {ECO:0000250|UniProtKB:O76011};
DE   AltName: Full=Hair keratin, type I Ha4;
DE   AltName: Full=Keratin-34 {ECO:0000250|UniProtKB:O76011, ECO:0000312|EMBL:CAM22480.1};
DE            Short=K34;
GN   Name=Krt34 {ECO:0000312|MGI:MGI:1309994};
GN   Synonyms=Ha4 {ECO:0000303|PubMed:1689759},
GN   Krt1-4 {ECO:0000312|MGI:MGI:1309994};
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:0000305, ECO:0000312|PIR:A60777}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Hair {ECO:0000269|PubMed:1689759};
RX   PubMed=1689759; DOI=10.1111/1523-1747.ep12874436;
RA   Bertolino A.P., Checkla D.M., Heitner S., Freedberg I.M., Yu D.W.;
RT   "Differential expression of type I hair keratins.";
RL   J. Invest. Dermatol. 94:297-303(1990).
RN   [2] {ECO:0000312|EMBL:BAB29474.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB29474.1};
RC   TISSUE=Neonatal skin {ECO:0000312|EMBL:BAB29474.1};
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   [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] {ECO:0000312|EMBL:CAM22480.1}
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   [5] {ECO:0000305, ECO:0000312|EMBL:AAI25421.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC   -!- TISSUE SPECIFICITY: Expressed in the hair root in the hair shaft
CC       cuticle and cortex. {ECO:0000269|PubMed:1689759}.
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}.
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DR   EMBL; AK014631; BAB29474.1; -; mRNA.
DR   EMBL; AL592545; CAM22480.1; -; Genomic_DNA.
DR   EMBL; CH466662; EDL02589.1; -; Genomic_DNA.
DR   EMBL; BC125420; AAI25421.1; -; mRNA.
DR   EMBL; BC125446; AAI25447.1; -; mRNA.
DR   CCDS; CCDS25404.1; -.
DR   PIR; A60777; A60777.
DR   RefSeq; NP_081839.1; NM_027563.4.
DR   AlphaFoldDB; Q9D646; -.
DR   SMR; Q9D646; -.
DR   DIP; DIP-303N; -.
DR   STRING; 10090.ENSMUSP00000056622; -.
DR   PhosphoSitePlus; Q9D646; -.
DR   jPOST; Q9D646; -.
DR   PaxDb; 10090-ENSMUSP00000056622; -.
DR   PeptideAtlas; Q9D646; -.
DR   ProteomicsDB; 264870; -.
DR   Antibodypedia; 28834; 130 antibodies from 26 providers.
DR   DNASU; 16672; -.
DR   Ensembl; ENSMUST00000056362.3; ENSMUSP00000056622.3; ENSMUSG00000043485.3.
DR   GeneID; 16672; -.
DR   KEGG; mmu:16672; -.
DR   UCSC; uc007lkc.1; mouse.
DR   AGR; MGI:1309994; -.
DR   CTD; 3885; -.
DR   MGI; MGI:1309994; Krt34.
DR   VEuPathDB; HostDB:ENSMUSG00000043485; -.
DR   eggNOG; ENOG502RTXS; Eukaryota.
DR   GeneTree; ENSGT00940000163426; -.
DR   HOGENOM; CLU_012560_8_0_1; -.
DR   InParanoid; Q9D646; -.
DR   OMA; HHIHLYR; -.
DR   OrthoDB; 4640531at2759; -.
DR   PhylomeDB; Q9D646; -.
DR   TreeFam; TF332742; -.
DR   Reactome; R-MMU-6805567; Keratinization.
DR   Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR   BioGRID-ORCS; 16672; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Krt33b; mouse.
DR   PRO; PR:Q9D646; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q9D646; Protein.
DR   Bgee; ENSMUSG00000043485; Expressed in lip and 13 other cell types or tissues.
DR   Genevisible; Q9D646; MM.
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.
PE   2: Evidence at transcript level;
KW   Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           1..392
FT                   /note="Keratin, type I cuticular Ha4"
FT                   /id="PRO_0000361023"
FT   DOMAIN          56..367
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..56
FT                   /note="Head"
FT   REGION          57..91
FT                   /note="Coil 1A"
FT   REGION          92..102
FT                   /note="Linker 1"
FT   REGION          103..203
FT                   /note="Coil 1B"
FT   REGION          204..219
FT                   /note="Linker 12"
FT   REGION          220..363
FT                   /note="Coil 2"
FT   REGION          364..392
FT                   /note="Tail"
FT   SITE            275
FT                   /note="Stutter"
SQ   SEQUENCE   392 AA;  44560 MW;  F466835182AFFB32 CRC64;
     MSCESCLPAL SCRTSCSSRP CVPPSCHGCT LPGACNIPAN VGNCNWFCEG SFNGNEKETM
     QFLNDRLASY MEKVRQLERE NAELECRIQE RNQQQDPLVC PAYQAYFRTI EELQQKILCA
     KSENARLVVQ IDNAKLASDD FRTKYQTELS MRQLVEADIN SLRRILDELT LCKSDLEAQV
     ESLREELLCL KKNHEEEVNT LRCQLGDRLN VEVDAAPTVD LNRVLNETRC QYEALVETNR
     REVEEWFTTQ SEELNKQVVS SSEQLQSCQA EIIELRRTVN ALEIELQAQH CMRNSLENTL
     TESEARYSSQ LSQVQCLITN VESQLGEIRA DLERQNQEYQ VLLDVRARLE CEINTYRSLL
     ESEDCNLPCN PCATTNASGS CCGPCGSSKR CC
//
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