KR192_MOUSE
ID KR192_MOUSE Reviewed; 141 AA.
AC Q925I0; Q3UUY7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Keratin-associated protein 19-2;
DE AltName: Full=Keratin-associated protein 16-1;
DE AltName: Full=Keratin-associated protein 16.1 {ECO:0000312|EMBL:AAK52889.1};
GN Name=Krtap19-2;
GN Synonyms=Krtap16-1, Krtap16.1 {ECO:0000312|EMBL:AAK52889.1};
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|EMBL:AAK52889.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=FVB/NJ {ECO:0000312|EMBL:AAK52889.1};
RC TISSUE=Skin {ECO:0000269|PubMed:11290294};
RX PubMed=11290294; DOI=10.1242/dev.128.9.1547;
RA Tkatchenko A.V., Visconti R.P., Shang L., Papenbrock T., Pruett N.D.,
RA Ito T., Ogawa M., Awgulewitsch A.;
RT "Overexpression of Hoxc13 in differentiating keratinocytes results in
RT downregulation of a novel hair keratin gene cluster and alopecia.";
RL Development 128:1547-1558(2001).
RN [2] {ECO:0000312|EMBL:AAI15788.1}
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).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAE23486.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 98-141.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23486.1};
RC TISSUE=Neonatal skin {ECO:0000312|EMBL:BAE23486.1};
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 [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=15385554; DOI=10.1074/jbc.m404331200;
RA Pruett N.D., Tkatchenko T.V., Jave-Suarez L., Jacobs D.F., Potter C.S.,
RA Tkatchenko A.V., Schweizer J., Awgulewitsch A.;
RT "Krtap16, characterization of a new hair keratin-associated protein (KAP)
RT gene complex on mouse chromosome 16 and evidence for regulation by
RT Hoxc13.";
RL J. Biol. Chem. 279:51524-51533(2004).
RN [5] {ECO:0000305}
RP INDUCTION.
RX PubMed=17151017; DOI=10.1242/dev.02721;
RA Kurek D., Garinis G.A., van Doorninck J.H., van der Wees J., Grosveld F.G.;
RT "Transcriptome and phenotypic analysis reveals Gata3-dependent signalling
RT pathways in murine hair follicles.";
RL Development 134:261-272(2007).
CC -!- FUNCTION: In the hair cortex, hair keratin intermediate filaments are
CC embedded in an interfilamentous matrix, consisting of hair keratin-
CC associated proteins (KRTAP), which are essential for the formation of a
CC rigid and resistant hair shaft through their extensive disulfide bond
CC cross-linking with abundant cysteine residues of hair keratins. The
CC matrix proteins include the high-sulfur and high-glycine-tyrosine
CC keratins. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with hair keratins. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strong expression in narrowly defined pattern
CC restricted to the lower and middle cortical regions of the hair shaft
CC in both developing and cycling hair. During hair follicle regression
CC (catagen), expression levels decrease until expression is no longer
CC detectable in follicles at resting stage (telogen).
CC {ECO:0000269|PubMed:15385554}.
CC -!- INDUCTION: Expression in skin and hair follicle is regulated by HOXC13
CC and by GATA3. {ECO:0000269|PubMed:11290294,
CC ECO:0000269|PubMed:17151017}.
CC -!- SIMILARITY: Belongs to the KRTAP type 19 family. {ECO:0000305}.
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DR EMBL; AF345291; AAK52889.1; -; mRNA.
DR EMBL; BC115787; AAI15788.1; -; mRNA.
DR EMBL; BC115815; AAI15816.1; -; mRNA.
DR EMBL; AK137740; BAE23486.1; -; mRNA.
DR CCDS; CCDS28304.1; -.
DR RefSeq; NP_570940.1; NM_130870.1.
DR AlphaFoldDB; Q925I0; -.
DR STRING; 10090.ENSMUSP00000075543; -.
DR PaxDb; Q925I0; -.
DR PRIDE; Q925I0; -.
DR ProteomicsDB; 263565; -.
DR Ensembl; ENSMUST00000076186; ENSMUSP00000075543; ENSMUSG00000057650.
DR GeneID; 170651; -.
DR KEGG; mmu:170651; -.
DR UCSC; uc007zvi.1; mouse.
DR CTD; 337969; -.
DR MGI; MGI:2157572; Krtap19-2.
DR VEuPathDB; HostDB:ENSMUSG00000057650; -.
DR GeneTree; ENSGT00950000184870; -.
DR HOGENOM; CLU_1824686_0_0_1; -.
DR OMA; GGGYPRY; -.
DR Reactome; R-MMU-6805567; Keratinization.
DR BioGRID-ORCS; 170651; 0 hits in 17 CRISPR screens.
DR PRO; PR:Q925I0; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q925I0; protein.
DR Bgee; ENSMUSG00000057650; Expressed in lip and 9 other tissues.
DR Genevisible; Q925I0; MM.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR InterPro; IPR021743; KRTAP_type6/8/16/19/20/21.
DR Pfam; PF11759; KRTAP; 1.
PE 2: Evidence at transcript level;
KW Keratin; Reference proteome; Repeat.
FT CHAIN 1..141
FT /note="Keratin-associated protein 19-2"
FT /id="PRO_0000356212"
FT REGION 5..135
FT /note="48 X 2 AA repeats of G-[YCGS]"
FT /evidence="ECO:0000255"
SQ SEQUENCE 141 AA; 13738 MW; EF58E63AD0BEF3E0 CRC64;
MSYYSGYSGG LGYGYGSSFG GLGCGCNSIR RLGCGSGYGG FGYGSGYGGF GGFGYGSGYG
GYGYGSGYGG FGGFGYGSGY GGFGYGSGYG GFGGFGYGSG YGGYGYGSGF GGYGYGSGFR
GYGCGCRRSS CCGGYGFSSF Y
