K1C19_PONAB
ID K1C19_PONAB Reviewed; 400 AA.
AC Q5R8S9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
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 {ECO:0000250|UniProtKB:P08727};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH91831.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:CAH91831.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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|UniProtKB:P08727, ECO:0000305}.
CC -!- DOMAIN: This keratin differs from all other IF proteins in lacking the
CC C-terminal tail domain. {ECO:0000305}.
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; CR859670; CAH91831.1; -; mRNA.
DR RefSeq; NP_001126058.1; NM_001132586.2.
DR AlphaFoldDB; Q5R8S9; -.
DR SMR; Q5R8S9; -.
DR STRING; 9601.ENSPPYP00000009462; -.
DR PRIDE; Q5R8S9; -.
DR GeneID; 100173010; -.
DR KEGG; pon:100173010; -.
DR CTD; 3880; -.
DR eggNOG; ENOG502QV0B; Eukaryota.
DR InParanoid; Q5R8S9; -.
DR OrthoDB; 798081at2759; -.
DR Proteomes; UP000001595; Unplaced.
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;
KW Reference proteome.
FT CHAIN 1..400
FT /note="Keratin, type I cytoskeletal 19"
FT /evidence="ECO:0000305"
FT /id="PRO_0000227526"
FT DOMAIN 80..391
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..79
FT /note="Head"
FT /evidence="ECO:0000255"
FT REGION 80..115
FT /note="Coil 1A"
FT /evidence="ECO:0000255"
FT REGION 116..133
FT /note="Linker 1"
FT /evidence="ECO:0000255"
FT REGION 134..225
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 226..248
FT /note="Linker 12"
FT /evidence="ECO:0000255"
FT REGION 244..390
FT /note="Necessary for interaction with PNN"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT REGION 249..387
FT /note="Coil 2"
FT /evidence="ECO:0000255"
FT REGION 388..400
FT /note="Rod-like helical tail"
FT /evidence="ECO:0000255"
FT SITE 267
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT SITE 327
FT /note="Stutter"
FT /evidence="ECO:0000255"
FT MOD_RES 7
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 22
FT /note="Phosphoserine"
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 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63279"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 51
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63279"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19001"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 391
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08727"
SQ SEQUENCE 400 AA; 44065 MW; F79117D835502118 CRC64;
MTSYSYRQSS AMSSFGGLGG GSVRFGPGVA FRAPSIHGGS GGRGVSVSSA RFVSSSSSGG
YGGGYGGVLT ASDGLLAGNE KLTMQNLNDR LASYLDKVRA LEAANGELEV KIRDWYQKQG
PGPSRDYSHY YTTIQDLRDK ILGATIENSR IVLQIDNARL AADDFRTKFE TEQALRMSVE
ADINGLRRVL DELTLARADL EMQIEGLKEE LAYLKKNHEE EISTLRGQVG GQVSVEVDSA
PGTDLAKILS DMRSQYEVMA EQNRKDAEAW FTSRTEELNR EVAGHTEQLQ MSRSEVTDLR
RTLQGLEIEL QSQLSMKAAL EDTLAETEAR FGAQLAHIQA LISGIEAQLG DVRADSERQN
QEYQRLMDIK SRLEQEIATY RSLLEGQEDH YSNLSASKVL
