ID   K2C3_RABIT              Reviewed;         629 AA.
AC   Q29426;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Keratin, type II cytoskeletal 3;
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=7691837; DOI=10.1242/jcs.105.2.303;
RA   Wu R.L., Galvin S., Wu S.K., Xu C., Blumenberg M., Sun T.T.;
RT   "A 300 bp 5'-upstream sequence of a differentiation-dependent rabbit K3
RT   keratin gene can serve as a keratinocyte-specific promoter.";
RL   J. Cell Sci. 105:303-316(1993).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=14638708; DOI=10.1167/iovs.03-0584;
RA   Espana E.M., Kawakita T., Romano A., Di Pascuale M., Smiddy R., Liu C.Y.,
RA   Tseng S.C.;
RT   "Stromal niche controls the plasticity of limbal and corneal epithelial
RT   differentiation in a rabbit model of recombined tissue.";
RL   Invest. Ophthalmol. Vis. Sci. 44:5130-5135(2003).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Keratin-3 associates with keratin-12.
CC   -!- TISSUE SPECIFICITY: Cornea specific. Expressed in the basal cells of
CC       corneal epithelium and stroma. Also expressed in esophageal epithelium.
CC       {ECO:0000269|PubMed:14638708, ECO:0000269|PubMed:7691837}.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; S65740; AAB28323.1; -; Genomic_DNA.
DR   EMBL; X74371; CAA52409.1; -; Genomic_DNA.
DR   PIR; S42629; S42629.
DR   RefSeq; XP_002711051.1; XM_002711005.2.
DR   AlphaFoldDB; Q29426; -.
DR   SMR; Q29426; -.
DR   STRING; 9986.ENSOCUP00000008551; -.
DR   PRIDE; Q29426; -.
DR   Ensembl; ENSOCUT00000009929; ENSOCUP00000008551; ENSOCUG00000029194.
DR   GeneID; 100353668; -.
DR   KEGG; ocu:100353668; -.
DR   CTD; 3850; -.
DR   eggNOG; ENOG502QURK; Eukaryota.
DR   GeneTree; ENSGT00940000162629; -.
DR   InParanoid; Q29426; -.
DR   OrthoDB; 824246at2759; -.
DR   Proteomes; UP000001811; Chromosome 4.
DR   Bgee; ENSOCUG00000029194; Expressed in skin of back and 3 other tissues.
DR   ExpressionAtlas; Q29426; baseline.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF16208; Keratin_2_head; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   SMART; SM01391; Filament; 1.
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; Methylation; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..629
FT                   /note="Keratin, type II cytoskeletal 3"
FT                   /id="PRO_0000063717"
FT   DOMAIN          183..498
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..182
FT                   /note="Head"
FT   REGION          183..218
FT                   /note="Coil 1A"
FT   REGION          219..239
FT                   /note="Linker 1"
FT   REGION          240..331
FT                   /note="Coil 1B"
FT   REGION          332..355
FT                   /note="Linker 12"
FT   REGION          356..494
FT                   /note="Coil 2"
FT   REGION          495..629
FT                   /note="Tail"
FT   REGION          603..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..629
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04264"
FT   MOD_RES         62
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04264"
FT   MOD_RES         281
FT                   /note="N6,N6-dimethyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P04264"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P04264"
SQ   SEQUENCE   629 AA;  64341 MW;  A4F456D366AC1A72 CRC64;
     MNRQVCKTSG GGSLSFSGRS AVVSGSGGGG SSSRMSCVAR SVAAGGGASG FRGGAGGFGS
     RSLYNLGGHK SISMSVAAGG SRAGGFGGGR SICGSGFGGG LGGGLGGGLG SGFGGGFGGG
     FGGAGAFGGA GGFGGAGGFG GPGGFGGPGG FPGGIQEVTV NQSLLQPLNV EIDPQIGQVR
     AQEREQIKTL NNKFASFIDK VRFLEQQNKV LETKWELLQR QGPNSVTGTN NLEPLFENRI
     NYLRSYLDSI VGERGRLDSE LRSMQDLVED FKKKYEDEIN KRTAAENEFV TLKKDVDAAY
     MNKVELQAKV DSLMDEINFL RTLYDAELSQ MQSHVSDMSV VLSMDNNRSL DLDSIIAEVR
     AQYEDIAQRS RAEAEAWYQT KLGELQTTAG RHGDDLRSTK NEIAEINRMI QRLRNEIENV
     KKQNASLQTA IAEAEQRGEL ALKDANAKLQ ELQAALQQAK DDLARLLRDY QELMNVKLAL
     DVEIATYRKL LEGEESRMSG ECQSAVSISV VNSSSTTSAA AGGYGGGYGG GYGGGFGVGG
     GAGSGFGRGG GSGFGGGSGL GGGSGFGGGS GLGGGSGLGG GSIGFSVGSS GFGSGSGGRI
     GVSGGGFSSG SSSRGSSVKF SQSSQRYSR