HORN_MOUSE
ID HORN_MOUSE Reviewed; 2496 AA.
AC Q8VHD8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Hornerin;
GN Name=Hrnr;
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 [MRNA].
RC STRAIN=ICR;
RX PubMed=11572870; DOI=10.1074/jbc.m107512200;
RA Makino T., Takaishi M., Morohashi M., Huh N.-H.;
RT "Hornerin, a novel profilaggrin-like protein and differentiation-specific
RT marker isolated from mouse skin.";
RL J. Biol. Chem. 276:47445-47452(2001).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=12642627; DOI=10.1177/002215540305100410;
RA Makino T., Takaishi M., Toyoda M., Morohashi M., Huh N.-H.;
RT "Expression of hornerin in stratified squamous epithelium in the mouse: a
RT comparative analysis with profilaggrin.";
RL J. Histochem. Cytochem. 51:485-492(2003).
RN [3]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-646; ARG-995; ARG-1343; ARG-1691;
RP ARG-2039; ARG-2210 AND ARG-2381, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Component of the epidermal cornified cell envelopes.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Found in keratohyalin
CC granules of the granular cells of the epidermis.
CC -!- TISSUE SPECIFICITY: Embryonic skin. Highest level in the adult
CC forestomach followed by the skin. Lower levels in the tongue,
CC esophagus. Detected in the granular and cornified layers of the mature
CC epidermis. {ECO:0000269|PubMed:12642627}.
CC -!- DEVELOPMENTAL STAGE: First detected on gestational day 15.5 in the
CC epidermis.
CC -!- PTM: Processed during the process of epidermal differentiation.
CC -!- PTM: Forms covalent cross-links mediated by transglutaminase TGM3,
CC between glutamine and the epsilon-amino group of lysine residues (in
CC vitro). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S100-fused protein family. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the S-100 family.
CC {ECO:0000305}.
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DR EMBL; AY027660; AAK15791.1; -; mRNA.
DR AlphaFoldDB; Q8VHD8; -.
DR SMR; Q8VHD8; -.
DR STRING; 10090.ENSMUSP00000088369; -.
DR iPTMnet; Q8VHD8; -.
DR PhosphoSitePlus; Q8VHD8; -.
DR CPTAC; non-CPTAC-4039; -.
DR MaxQB; Q8VHD8; -.
DR PaxDb; Q8VHD8; -.
DR PRIDE; Q8VHD8; -.
DR ProteomicsDB; 273188; -.
DR MGI; MGI:3046938; Hrnr.
DR eggNOG; ENOG502QQH0; Eukaryota.
DR InParanoid; Q8VHD8; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR PRO; PR:Q8VHD8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VHD8; protein.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0036457; C:keratohyalin granule; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0043163; P:cell envelope organization; ISO:MGI.
DR GO; GO:0061436; P:establishment of skin barrier; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR CDD; cd00213; S-100; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR033201; HRNR.
DR InterPro; IPR034325; S-100_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR PANTHER; PTHR22571:SF25; PTHR22571:SF25; 8.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Calcium; Developmental protein; Keratinization; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2496
FT /note="Hornerin"
FT /id="PRO_0000144039"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 49..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 99..145
FT /note="1; truncated"
FT REPEAT 146..231
FT /note="2"
FT REPEAT 232..321
FT /note="3"
FT REPEAT 326..400
FT /note="4"
FT REPEAT 401..491
FT /note="5"
FT REPEAT 492..577
FT /note="6"
FT REPEAT 578..668
FT /note="7"
FT REPEAT 669..748
FT /note="8"
FT REPEAT 749..839
FT /note="9"
FT REPEAT 840..926
FT /note="10"
FT REPEAT 927..1017
FT /note="11"
FT REPEAT 1018..1097
FT /note="12"
FT REPEAT 1098..1188
FT /note="13"
FT REPEAT 1189..1274
FT /note="14"
FT REPEAT 1275..1365
FT /note="15"
FT REPEAT 1366..1445
FT /note="16"
FT REPEAT 1446..1536
FT /note="17"
FT REPEAT 1537..1622
FT /note="18"
FT REPEAT 1623..1713
FT /note="19"
FT REPEAT 1714..1793
FT /note="20"
FT REPEAT 1794..1884
FT /note="21"
FT REPEAT 1885..1970
FT /note="22"
FT REPEAT 1971..2061
FT /note="23"
FT REPEAT 2062..2141
FT /note="24"
FT REPEAT 2142..2232
FT /note="25"
FT REPEAT 2233..2312
FT /note="26"
FT REPEAT 2313..2403
FT /note="27"
FT REPEAT 2410..2496
FT /note="28"
FT REGION 1..81
FT /note="S-100-like"
FT REGION 82..98
FT /note="S (spacer)"
FT REGION 97..2496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..2496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 646
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 995
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 1343
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1551
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 1553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 1650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 1691
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2011
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 2039
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 2124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 2210
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YZ3"
FT MOD_RES 2381
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 2496 AA; 247587 MW; 4CE136CA6CE657DE CRC64;
MPKLLESIVT VIDVFYQYAT EYGNCDMLSK EEMKELLVTE FHQILKNPDD PDTVDIIMQN
LDRDHNHKVD FTEYLLMILK LTKACNKIIG KDYCQASGSK QKNHSHQHQE EQSKKETENK
EQKGSISSSA GENDSYSRGS RGSNKSKSKK LRKGKEQSSK QTTKSNSSDH ENSEDYEQGQ
HESGFSNSSG NGRPSSRKAS GFPQPGSEQG QSSSSSTKGS GECYSSGNGK HGSSSGGSAV
SGSGHSNTYG KQGTGSRHSS SNRRSRSTSR ESSGSQEYSS GSSEEPGFTH GSGRKNSSTC
GKNGSYSGQS TGRHQQGFGS SHELESGQSI TSANHGSHSN QSSCSGTREC GSSESSMKKT
HVSGSGHSSS TGKYTSTSGQ NYNSTRQGCG QGKSSGSEQY GASSGQSSGC SSGQSTRYGE
QGSGSRNSST QSRGRSTSRE SSTSQQFGSG SGRSSGFSQG GSGQGRSSRG GQQGSFSGQT
EGSQQHGSCC GQSSGYGQNE YGSGHSASSG QQGSHYSQSS SYGTHNSGGS PSSSQRGHGS
RSGRSSGLGQ YGSPSGQTSS STRQGSGQGQ ASGSGRYGAS SGQTSGCGSG QSTRYGEQGS
GSRNSSTQSR GRSTSRESST SQRYGSGSGE SSGFSQGGSG QGRSSRGGQQ GSFSGQTSGR
SQHQSGSRHG SGSGQFPISG QQGSHHGHSS SSGTHNSGSS QSSSTQWSHG SGSEQSSGLG
HYGSTSGQTA SSTRQGSGQG QASGSGRCGA SSGQTSGCGS GQSTRYGEQG SGSRNSSTQS
RGRSTSRESS TSQRFGSGSG GSSGFSQGRS GQGRSSRGGQ QGSFSGQTEG SQQHGSCCGQ
SSGYGQNEYG SGHSASSGQQ GSHYSQSSSY GTHNSGGSPS SRPAGGHGSR SGRSSGLGQY
GSPSGQTSSS TRQGSGQGQA SGSGRYGASS GQTSGCGSGQ STRYGEQGSG SRNSSTQSRG
RSTSRESSTS QRYGSGSGES SGFSQGGSGQ GRSSRGGQQG SFSGQTSGRS QHQSGSRHGS
GSGQFPISGQ QGSHHGHSSS SGTHNSGSSQ SSSTQWSHGS GSEQSSGLGH YGSTSGQTAS
STRQGSGQGQ ASGSGRCGAS SGQTSGCGSG QSTRYGEQGS GSRNSSTQSR GRSTSRESST
SQRFGSGSGG SSGFSQGRSG QGRSSRGGQQ GSFSGQTEGS QQHGSCCGQS SGYGQNEYGS
GHSASSGQQG SHYSQSSSYG THNSGGSPSS SQRGHGSRSG RSSGLGQYGS PSGQTSSSTR
QGSGQGQASG SGRYGASSGQ TSGCRSGQST RYGGQGSGSR NSSTQSRGRS TSRESSTSQR
YGSGSGESSG FSQGGSGQGR SSRGGQQGSF SGQTSGRNQH QSGSRHGSGS GQFPISGQQG
SHHGHSSSSG THNSGSSQSS STQWSHGSGS EQSSGLGHYG STSGQTASST RQGSGQGQAS
GSGRCGASSG QTSGCGSGQS TRYGEQGSGS RNSSTQSRGR STSRESSTSQ RFGSGSGGSS
GFSQGRSGQG RSSRGGQQGS FSGQTEGSQQ HGSCCGQSSG YGQNEYGSGH SASSGQQGSH
YSQSSSYGTH NSGGSPSSSQ RGHGSRSGRS SGLGQYGSPS GQTSSSTRQG SGQGQASGSG
RYGASSGQTS GCGSGQPTRY GEQGSGSRNS STQSRGRSTS RESSTSQRCG SGSGESSGFS
QGGSGQGRSS RGGQQGSFSG QTSGRSQHQS GSRHGSGSGQ FPISGQQGSH HGHSSSSGTH
NSGSSQSSST QWSHGSGSEQ SSGLGHYGST SGQTASSTRQ GSGQGQASGS GRCGASSGQT
SGCGSDQSTR YGEQGSGSRN SSTQSRGRST SRESSTSQRF GSGSGGSSGF SQGRSGQGRS
SRGGQQGSFS GQTEGSQQHG SCCGQSSGYG QNEYGSGHSA SSGQQGSHYS QSSSYGTHNS
GGSPSSSQRG HGSRSGRSSG LGQYGSPSGQ TSSSTRQGSG QGQASGSGRY GASSGQTSGC
GSGQSTRYGE QGSGSRNSST QSRGRSTSRE SSTSQRYGSG SGESSGFSQG GSGQGRSSRG
GQQGSFSGQT SGRSQHQSGS RHGSGSGQFP ISGQQGSHHG HSSSSGTHNS GSSQSSSTQW
SHGSGSEQSS GLGHYGSTSG QTASSTRQGS GQGQASGSGR CGASSGQTSG CGSGQSTRYG
EQGSGSRNSS TQSRGRSTSR ESSTSQRYGS GSGESSGFSQ GGSGQGRSSR GGQQGSFSGQ
TSGRSQHQSG SRHGSGSGQF PISGQQGSHH GHSSSSGTHN SGSSQSSSTQ WSHGSGSEQS
SGLGQYGSPS GQTSSSTRQG SGQGQASGSG RYGASSGQTS GCGSGQSTRY GEQGSGSRNS
STQSRGRSTS RESSTSQRYG SGSGESSGFS QGGSGQGRSS RGGQQGSFSG QTSGRSQHQS
GSRHGSGSGQ FPISGQQGSH HGHSSSSGTH NSGSSQSSST QWSHGSGSEQ SSGLGHYGST
SGQTASSTRQ GSGQGQASGS GRCGASSGQT SGCGSG
