ID   K1C19_POTTR             Reviewed;         401 AA.
AC   P51856;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Keratin, type I cytoskeletal 19;
DE   AltName: Full=Cytokeratin-19;
DE            Short=CK-19;
DE   AltName: Full=Keratin-19;
DE            Short=K19;
GN   Name=KRT19;
OS   Potorous tridactylus (Potoroo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Potoroidae; Potorous.
OX   NCBI_TaxID=9310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7543411; DOI=10.1111/j.1432-1033.1995.tb20721.x;
RA   Boettger V., Stasiak P.C., Harrison D.L., Mellerick D.M., Lane E.B.;
RT   "Epitope mapping of monoclonal antibodies to keratin 19 using keratin
RT   fragments, synthetic peptides and phage peptide libraries.";
RL   Eur. J. Biochem. 231:475-485(1995).
CC   -!- FUNCTION: Involved in the organization of myofibers. Together with
CC       KRT8, helps to link the contractile apparatus to dystrophin at the
CC       costameres of striated muscle (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Interacts with PNN and the actin-binding domain of DMD (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: This keratin differs from all other IF proteins in lacking the
CC       C-terminal tail domain.
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; X82579; CAA57915.1; -; mRNA.
DR   PIR; S66257; S57657.
DR   AlphaFoldDB; P51856; -.
DR   SMR; P51856; -.
DR   PRIDE; P51856; -.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; PTHR23239; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
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.
FT   CHAIN           1..401
FT                   /note="Keratin, type I cytoskeletal 19"
FT                   /id="PRO_0000063673"
FT   DOMAIN          80..391
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..79
FT                   /note="Head"
FT   REGION          80..115
FT                   /note="Coil 1A"
FT   REGION          116..133
FT                   /note="Linker 1"
FT   REGION          134..225
FT                   /note="Coil 1B"
FT   REGION          226..248
FT                   /note="Linker 12"
FT   REGION          244..390
FT                   /note="Necessary for interaction with PNN"
FT                   /evidence="ECO:0000250"
FT   REGION          249..387
FT                   /note="Coil 2"
FT   REGION          388..401
FT                   /note="Rod-like helical tail"
FT   SITE            267
FT                   /note="Stutter"
FT   SITE            327
FT                   /note="Stutter"
FT   MOD_RES         7
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P08727"
FT   MOD_RES         24
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08727"
FT   MOD_RES         24
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08727"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63279"
FT   MOD_RES         31
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P08727"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P08727"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q63279"
FT   MOD_RES         48
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P08727"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19001"
FT   MOD_RES         323
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P08727"
SQ   SEQUENCE   401 AA;  43830 MW;  B87D37F0EB7ED938 CRC64;
     MTSYSYRQSS STSTLGLGSN NAARFGSGAF RAPSIHGGSG GLGVSVSRFA SSGLSGGYGG
     GSSSFSVGYG GADGLLAGNE KITMQNLNDR LASYLDKVRA LEEANADLEV KIRDWCQKQG
     PGPARDYSAY MTTIQDLRDK ILGATIENSK IVLQIDNARL AADDFRTKFE TEEALRLSVE
     ADINGLRRVL DELTLARADL EMQIEGLKEE LAYLKKNHEE EISALSGQVG GQVSVEVDSA
     PGIDLAKILT DMRSQYEAMV EKNRSDAEAW FTSKTDELNQ EVAVHTKLLQ TSKTEVTDLR
     RTLQGLEIEL QSQLSMKAAL EGTLAETEAR YGVQLSQIQA LISNIESQLS DIRADMERQN
     QEYLLLMDIK SRLEREIATY RSLLEGHDAQ DNIVPTTPKA L