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Keratin, type II cytoskeletal 3 (65 kDa cytokeratin) (Cytokeratin-3) (CK-3) (Keratin-3) (K3) (Type-II keratin Kb3)

 K2C3_HUMAN              Reviewed;         628 AA.
P12035; A6NIS2; Q701L8;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 3.
28-FEB-2018, entry version 171.
RecName: Full=Keratin, type II cytoskeletal 3;
AltName: Full=65 kDa cytokeratin;
AltName: Full=Cytokeratin-3;
Short=CK-3;
AltName: Full=Keratin-3;
Short=K3;
AltName: Full=Type-II keratin Kb3;
Name=KRT3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-375.
PubMed=2439698; DOI=10.1007/BF02134130;
Klinge E.M., Sylvestre Y.R., Freedberg I.M., Blumenberg M.;
"Evolution of keratin genes: different protein domains evolve by
different pathways.";
J. Mol. Evol. 24:319-329(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-628.
TISSUE=Eye;
PubMed=15737194; DOI=10.1111/j.0022-202X.2004.23530.x;
Rogers M.A., Edler L., Winter H., Langbein L., Beckmann I.,
Schweizer J.;
"Characterization of new members of the human type II keratin gene
family and a general evaluation of the keratin gene domain on
chromosome 12q13.13.";
J. Invest. Dermatol. 124:536-544(2005).
[4]
VARIANT MECD LYS-509.
PubMed=9171831; DOI=10.1038/ng0697-184;
Irvine A.D., Corden L.D., Swensson O., Swensson B., Moore J.E.,
Frazer D.G., Smith F.J.D., Knowlton R.G., Christophers E., Rochels R.,
Uitto J., McLean W.H.I.;
"Mutations in cornea-specific keratin K3 or K12 genes cause Meesmann's
corneal dystrophy.";
Nat. Genet. 16:184-187(1997).
[5]
VARIANT MECD PRO-503.
PubMed=16227835; DOI=10.1097/01.ico.0000159732.29930.26;
Chen Y.T., Tseng S.H., Chao S.C.;
"Novel mutations in the helix termination motif of keratin 3 and
keratin 12 in 2 Taiwanese families with Meesmann corneal dystrophy.";
Cornea 24:928-932(2005).
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
Keratin-3 associates with keratin-12.
-!- INTERACTION:
O14964:HGS; NbExp=4; IntAct=EBI-2430095, EBI-740220;
O76013-2:KRT36; NbExp=4; IntAct=EBI-2430095, EBI-11958506;
-!- TISSUE SPECIFICITY: Cornea specific.
-!- DISEASE: Corneal dystrophy, Meesmann (MECD) [MIM:122100]: An
autosomal dominant corneal disease characterized by fragility of
the anterior corneal epithelium. Patients are usually asymptomatic
until adulthood when rupture of the corneal microcysts may cause
erosions, producing clinical symptoms such as photophobia, contact
lens intolerance and intermittent diminution of visual acuity.
Rarely, subepithelial scarring causes irregular corneal
astigmatism and permanent visual impairment. Histological
examination shows a disorganized and thickened epithelium with
widespread cytoplasmic vacuolation and numerous small, round,
debris-laden intraepithelial cysts. {ECO:0000269|PubMed:16227835,
ECO:0000269|PubMed:9171831}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- SEQUENCE CAUTION:
Sequence=CAF31522.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
-!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-3 entry;
URL="https://en.wikipedia.org/wiki/Keratin_3";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X05418; CAA28991.1; -; Genomic_DNA.
EMBL; X05419; CAA28992.1; -; Genomic_DNA.
EMBL; X05420; CAA28993.1; -; Genomic_DNA.
EMBL; X05420; CAA28994.1; -; Genomic_DNA.
EMBL; X05420; CAA28995.1; -; Genomic_DNA.
EMBL; X05421; CAA28996.1; -; Genomic_DNA.
EMBL; AC107016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ628418; CAF31522.1; ALT_INIT; mRNA.
CCDS; CCDS44895.1; -.
PIR; A29666; A29666.
RefSeq; NP_476429.2; NM_057088.2.
UniGene; Hs.680652; -.
ProteinModelPortal; P12035; -.
SMR; P12035; -.
BioGrid; 110048; 18.
IntAct; P12035; 41.
STRING; 9606.ENSP00000413479; -.
iPTMnet; P12035; -.
PhosphoSitePlus; P12035; -.
SwissPalm; P12035; -.
BioMuta; KRT3; -.
DMDM; 313104225; -.
PaxDb; P12035; -.
PeptideAtlas; P12035; -.
PRIDE; P12035; -.
DNASU; 3850; -.
Ensembl; ENST00000417996; ENSP00000413479; ENSG00000186442.
GeneID; 3850; -.
KEGG; hsa:3850; -.
UCSC; uc001say.4; human.
CTD; 3850; -.
DisGeNET; 3850; -.
EuPathDB; HostDB:ENSG00000186442.7; -.
GeneCards; KRT3; -.
H-InvDB; HIX0036742; -.
HGNC; HGNC:6440; KRT3.
MalaCards; KRT3; -.
MIM; 122100; phenotype.
MIM; 148043; gene.
neXtProt; NX_P12035; -.
OpenTargets; ENSG00000186442; -.
Orphanet; 98954; Meesmann corneal dystrophy.
PharmGKB; PA30228; -.
eggNOG; ENOG410IKBD; Eukaryota.
eggNOG; ENOG4111UGN; LUCA.
GeneTree; ENSGT00760000118796; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; P12035; -.
KO; K07605; -.
OMA; LFENHIN; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P12035; -.
TreeFam; TF332742; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
GeneWiki; Keratin_3; -.
GenomeRNAi; 3850; -.
PRO; PR:P12035; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000186442; -.
CleanEx; HS_KRT3; -.
Genevisible; P12035; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; NAS:UniProtKB.
GO; GO:0045095; C:keratin filament; TAS:UniProtKB.
GO; GO:0005198; F:structural molecule activity; IMP:UniProtKB.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:UniProtKB.
GO; GO:0031424; P:keratinization; TAS:Reactome.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 3.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 2.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Corneal dystrophy; Disease mutation;
Intermediate filament; Keratin; Methylation; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 628 Keratin, type II cytoskeletal 3.
/FTId=PRO_0000063716.
DOMAIN 198 513 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 197 Head.
REGION 198 233 Coil 1A.
REGION 234 254 Linker 1.
REGION 255 346 Coil 1B.
REGION 347 370 Linker 12.
REGION 371 509 Coil 2.
REGION 510 628 Tail.
COMPBIAS 10 169 Gly-rich.
COMPBIAS 536 612 Gly-rich.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P04264}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000250|UniProtKB:P04264}.
MOD_RES 296 296 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P04264}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000250|UniProtKB:P04264}.
VARIANT 44 44 G -> A (in dbSNP:rs28721426).
/FTId=VAR_061297.
VARIANT 375 375 R -> G (in dbSNP:rs3887954).
{ECO:0000269|PubMed:2439698}.
/FTId=VAR_056023.
VARIANT 503 503 R -> P (in MECD; dbSNP:rs60410063).
{ECO:0000269|PubMed:16227835}.
/FTId=VAR_031327.
VARIANT 509 509 E -> K (in MECD; dbSNP:rs57872071).
{ECO:0000269|PubMed:9171831}.
/FTId=VAR_003868.
CONFLICT 162 162 G -> A (in Ref. 1; CAA28991).
{ECO:0000305}.
CONFLICT 175 175 I -> T (in Ref. 1; CAA28991).
{ECO:0000305}.
CONFLICT 184 184 N -> K (in Ref. 1; CAA28991).
{ECO:0000305}.
CONFLICT 187 187 I -> T (in Ref. 1; CAA28991).
{ECO:0000305}.
CONFLICT 298 298 T -> Y (in Ref. 1; CAA28993).
{ECO:0000305}.
CONFLICT 397 397 L -> M (in Ref. 1; CAA28996).
{ECO:0000305}.
CONFLICT 409 409 D -> G (in Ref. 3; CAF31522).
{ECO:0000305}.
CONFLICT 448 448 E -> Q (in Ref. 1; CAA28996).
{ECO:0000305}.
CONFLICT 511 511 Y -> YS (in Ref. 1; CAA28996).
{ECO:0000305}.
CONFLICT 562 562 S -> I (in Ref. 1; CAA28996).
{ECO:0000305}.
CONFLICT 580 580 S -> T (in Ref. 1; CAA28996).
{ECO:0000305}.
SEQUENCE 628 AA; 64417 MW; 65FDB8CAA7F3C960 CRC64;
MSRQASKTSG GGSQGFSGRS AVVSGSSRMS CVAHSGGAGG GAYGFRSGAG GFGSRSLYNL
GGNKSISISV AAGGSRAGGF GGGRSSCAFA GGYGGGFGSG YGGGFGGGFG GGRGMGGGFG
GAGGFGGAGG FGGAGGFGGP GGFGGSGGFG GPGSLGSPGG FGPGGFPGGI QEVTINQSLL
QPLNVEIDPQ IGQVKAQERE QIKTLNNKFA SFIDKVRFLE QQNKVLETKW NLLQQQGTSS
ISGTNNLEPL FENHINYLRS YLDNILGERG RLDSELKNME DLVEDFKKKY EDEINKRTAA
ENEFVTLKKD VDSAYMNKVE LQAKVDALID EIDFLRTLYD AELSQMQSHI SDTSVVLSMD
NNRSLDLDSI IAEVRAQYED IAQRSKAEAE ALYQTKLGEL QTTAGRHGDD LRNTKSEIIE
LNRMIQRLRA EIEGVKKQNA NLQTAIAEAE QHGEMALKDA NAKLQELQAA LQQAKDDLAR
LLRDYQELMN VKLALDVEIA TYRKLLEGEE YRMSGECPSA VSISVVSSST TSASAGGYGG
GYGGGMGGGL GGGFSAGGGS GSGFGRGGGG GIGGGFGGGS SGFSGGSGFG SISGARYGVS
GGGFSSASNR GGSIKFSQSS QSSQRYSR


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