ID A0A452J7B3_9SAUR Unreviewed; 473 AA.
AC A0A452J7B3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Keratin, type I cytoskeletal 14 {ECO:0000256|ARBA:ARBA00040326};
DE AltName: Full=Cytokeratin-14 {ECO:0000256|ARBA:ARBA00041705};
DE AltName: Full=Keratin-14 {ECO:0000256|ARBA:ARBA00042490};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000036385.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000036385.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: The nonhelical tail domain is involved in promoting KRT5-
CC KRT14 filaments to self-organize into large bundles and enhances the
CC mechanical properties involved in resilience of keratin intermediate
CC filaments in vitro. {ECO:0000256|ARBA:ARBA00037229}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000256|RuleBase:RU000685}.
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DR AlphaFoldDB; A0A452J7B3; -.
DR STRING; 38772.ENSGAGP00000036385; -.
DR Ensembl; ENSGAGT00000041205.1; ENSGAGP00000036385.1; ENSGAGG00000025794.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1.
DR PANTHER; PTHR23239:SF368; KERATIN, TYPE I CYTOSKELETAL 14; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW ECO:0000256|RuleBase:RU000685}; Keratin {ECO:0000256|ARBA:ARBA00022744};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT DOMAIN 121..432
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT COILED 125..159
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 224..350
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 376..417
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 473 AA; 51597 MW; 709C7E8B416606CF CRC64;
MTTSVRQYSS STSLKGLGGL SGLGGGSTRV SSVNLGGPYR APSIHGGSGG FSVSSSRYVS
GVGSSLGGGY GGSYSSSFGG GYGGGLGGGY GGCLGGGLGG GYGVGFGGGF GGGDGILPAG
EKETMQNLND RLATYLDKVR ALEEANSDLE IKIKEWYKKQ GPSPDRDYSP YYRTIEDLRS
KILSATVDNA SLLLQIDNAR LTADDFRTKF ETEQALRMSV EADINGLRRV LDELTLARAD
LEMQIENLKE ELAYLKKNHE EEMKILRSQL GGDITVEMDA APGVDLTKIL ADMREQYESL
AEKNRKEAEQ WFYTQTEQLN REVAMNTEQL QSGKSEITEL RRTVQGLEIE LQSQLSMKAA
LEGTLAETEA RYGTQLAQLQ ALITSVEEQL AELRCDMERQ NHEYKILVDV KTRLEQEIAT
YRRLLEGEDA HIASQYALAK EASMTTRQVR TIVEEVQDGK VISSREQVHH SSR
//