ID K2C3_HUMAN Reviewed; 628 AA. AC P12035; A6NIS2; Q701L8; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 11-NOV-2015, entry version 152. DE RecName: Full=Keratin, type II cytoskeletal 3; DE AltName: Full=65 kDa cytokeratin; DE AltName: Full=Cytokeratin-3; DE Short=CK-3; DE AltName: Full=Keratin-3; DE Short=K3; DE AltName: Full=Type-II keratin Kb3; GN Name=KRT3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-375. RX PubMed=2439698; DOI=10.1007/BF02134130; RA Klinge E.M., Sylvestre Y.R., Freedberg I.M., Blumenberg M.; RT "Evolution of keratin genes: different protein domains evolve by RT different pathways."; RL J. Mol. Evol. 24:319-329(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-628. RC TISSUE=Eye; RX PubMed=15737194; DOI=10.1111/j.0022-202X.2004.23530.x; RA Rogers M.A., Edler L., Winter H., Langbein L., Beckmann I., RA Schweizer J.; RT "Characterization of new members of the human type II keratin gene RT family and a general evaluation of the keratin gene domain on RT chromosome 12q13.13."; RL J. Invest. Dermatol. 124:536-544(2005). RN [4] RP VARIANT MECD LYS-509. RX PubMed=9171831; DOI=10.1038/ng0697-184; RA Irvine A.D., Corden L.D., Swensson O., Swensson B., Moore J.E., RA Frazer D.G., Smith F.J.D., Knowlton R.G., Christophers E., Rochels R., RA Uitto J., McLean W.H.I.; RT "Mutations in cornea-specific keratin K3 or K12 genes cause Meesmann's RT corneal dystrophy."; RL Nat. Genet. 16:184-187(1997). RN [5] RP VARIANT MECD PRO-503. RX PubMed=16227835; DOI=10.1097/01.ico.0000159732.29930.26; RA Chen Y.T., Tseng S.H., Chao S.C.; RT "Novel mutations in the helix termination motif of keratin 3 and RT keratin 12 in 2 Taiwanese families with Meesmann corneal dystrophy."; RL Cornea 24:928-932(2005). CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins. CC Keratin-3 associates with keratin-12. CC -!- TISSUE SPECIFICITY: Cornea specific. CC -!- DISEASE: Corneal dystrophy, Meesmann (MECD) [MIM:122100]: An CC autosomal dominant corneal disease characterized by fragility of CC the anterior corneal epithelium. Patients are usually asymptomatic CC until adulthood when rupture of the corneal microcysts may cause CC erosions, producing clinical symptoms such as photophobia, contact CC lens intolerance and intermittent diminution of visual acuity. CC Rarely, subepithelial scarring causes irregular corneal CC astigmatism and permanent visual impairment. Histological CC examination shows a disorganized and thickened epithelium with CC widespread cytoplasmic vacuolation and numerous small, round, CC debris-laden intraepithelial cysts. {ECO:0000269|PubMed:16227835, CC ECO:0000269|PubMed:9171831}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- MISCELLANEOUS: There are two types of cytoskeletal and CC microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to CC basic; 56-70 kDa). CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAF31522.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database; CC URL="http://www.interfil.org"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-3 entry; CC URL="https://en.wikipedia.org/wiki/Keratin_3"; 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; X05418; CAA28991.1; -; Genomic_DNA. DR EMBL; X05419; CAA28992.1; -; Genomic_DNA. DR EMBL; X05420; CAA28993.1; -; Genomic_DNA. DR EMBL; X05420; CAA28994.1; -; Genomic_DNA. DR EMBL; X05420; CAA28995.1; -; Genomic_DNA. DR EMBL; X05421; CAA28996.1; -; Genomic_DNA. DR EMBL; AC107016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ628418; CAF31522.1; ALT_INIT; mRNA. DR CCDS; CCDS44895.1; -. DR PIR; A29666; A29666. DR RefSeq; NP_476429.2; NM_057088.2. DR UniGene; Hs.680652; -. DR ProteinModelPortal; P12035; -. DR SMR; P12035; 198-339, 366-508. DR BioGrid; 110048; 14. DR IntAct; P12035; 3. DR STRING; 9606.ENSP00000413479; -. DR PhosphoSite; P12035; -. DR BioMuta; KRT3; -. DR DMDM; 313104225; -. DR MaxQB; P12035; -. DR PaxDb; P12035; -. DR PRIDE; P12035; -. DR DNASU; 3850; -. DR Ensembl; ENST00000417996; ENSP00000413479; ENSG00000186442. DR GeneID; 3850; -. DR KEGG; hsa:3850; -. DR UCSC; uc001say.3; human. DR CTD; 3850; -. DR GeneCards; KRT3; -. DR H-InvDB; HIX0036742; -. DR HGNC; HGNC:6440; KRT3. DR MIM; 122100; phenotype. DR MIM; 148043; gene. DR neXtProt; NX_P12035; -. DR Orphanet; 98954; Meesmann corneal dystrophy. DR PharmGKB; PA30228; -. DR eggNOG; ENOG410IKBD; Eukaryota. DR eggNOG; ENOG4111UGN; LUCA. DR GeneTree; ENSGT00760000118796; -. DR HOGENOM; HOG000230976; -. DR HOVERGEN; HBG013015; -. DR InParanoid; P12035; -. DR KO; K07605; -. DR OMA; LFENHIN; -. DR OrthoDB; EOG7FV3Q8; -. DR PhylomeDB; P12035; -. DR TreeFam; TF332742; -. DR GeneWiki; Keratin_3; -. DR GenomeRNAi; 3850; -. DR NextBio; 15149; -. DR PRO; PR:P12035; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; P12035; -. DR CleanEx; HS_KRT3; -. DR Genevisible; P12035; HS. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005882; C:intermediate filament; NAS:UniProtKB. DR GO; GO:0045095; C:keratin filament; TAS:UniProtKB. DR GO; GO:0005198; F:structural molecule activity; IMP:UniProtKB. DR GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:UniProtKB. DR InterPro; IPR001664; IF. DR InterPro; IPR018039; Intermediate_filament_CS. DR InterPro; IPR032444; Keratin_2_head. DR InterPro; IPR003054; Keratin_II. DR PANTHER; PTHR23239; PTHR23239; 3. DR Pfam; PF00038; Filament; 1. DR Pfam; PF16208; Keratin_2_head; 2. DR PRINTS; PR01276; TYPE2KERATIN. DR PROSITE; PS00226; IF; 1. PE 1: Evidence at protein level; KW Coiled coil; Complete proteome; Corneal dystrophy; Disease mutation; KW Intermediate filament; Keratin; Methylation; Phosphoprotein; KW Polymorphism; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P04264}. FT CHAIN 2 628 Keratin, type II cytoskeletal 3. FT /FTId=PRO_0000063716. FT REGION 2 197 Head. FT REGION 198 509 Rod. FT REGION 198 233 Coil 1A. FT REGION 234 254 Linker 1. FT REGION 255 346 Coil 1B. FT REGION 347 370 Linker 12. FT REGION 371 509 Coil 2. FT REGION 510 628 Tail. FT COMPBIAS 10 169 Gly-rich. FT COMPBIAS 536 612 Gly-rich. FT MOD_RES 56 56 Phosphoserine. FT {ECO:0000250|UniProtKB:P04264}. FT MOD_RES 296 296 N6,N6-dimethyllysine. FT {ECO:0000250|UniProtKB:P04264}. FT MOD_RES 364 364 Phosphoserine. FT {ECO:0000250|UniProtKB:P04264}. FT VARIANT 44 44 G -> A (in dbSNP:rs28721426). FT /FTId=VAR_061297. FT VARIANT 375 375 R -> G (in dbSNP:rs3887954). FT {ECO:0000269|PubMed:2439698}. FT /FTId=VAR_056023. FT VARIANT 503 503 R -> P (in MECD; dbSNP:rs60410063). FT {ECO:0000269|PubMed:16227835}. FT /FTId=VAR_031327. FT VARIANT 509 509 E -> K (in MECD; dbSNP:rs57872071). FT {ECO:0000269|PubMed:9171831}. FT /FTId=VAR_003868. FT CONFLICT 162 162 G -> A (in Ref. 1; CAA28991). FT {ECO:0000305}. FT CONFLICT 175 175 I -> T (in Ref. 1; CAA28991). FT {ECO:0000305}. FT CONFLICT 184 184 N -> K (in Ref. 1; CAA28991). FT {ECO:0000305}. FT CONFLICT 187 187 I -> T (in Ref. 1; CAA28991). FT {ECO:0000305}. FT CONFLICT 298 298 T -> Y (in Ref. 1; CAA28993). FT {ECO:0000305}. FT CONFLICT 397 397 L -> M (in Ref. 1; CAA28996). FT {ECO:0000305}. FT CONFLICT 409 409 D -> G (in Ref. 3; CAF31522). FT {ECO:0000305}. FT CONFLICT 448 448 E -> Q (in Ref. 1; CAA28996). FT {ECO:0000305}. FT CONFLICT 511 511 Y -> YS (in Ref. 1; CAA28996). FT {ECO:0000305}. FT CONFLICT 562 562 S -> I (in Ref. 1; CAA28996). FT {ECO:0000305}. FT CONFLICT 580 580 S -> T (in Ref. 1; CAA28996). FT {ECO:0000305}. SQ 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 //