K1C1_CARAU
ID K1C1_CARAU Reviewed; 467 AA.
AC Q90303;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Keratin, type I cytoskeletal 50 kDa;
DE AltName: Full=GK50;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1283739; DOI=10.1111/j.1432-0436.1992.tb00497.x;
RA Druger R.K., Levine E.M., Glasgow E., Jones P.S., Schechter N.;
RT "Cloning of a type I keratin from goldfish optic nerve: differential
RT expression of keratins during regeneration.";
RL Differentiation 52:33-43(1992).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC -!- TISSUE SPECIFICITY: Optic nerve.
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; M86918; AAA49184.1; -; mRNA.
DR PIR; I50476; I50476.
DR AlphaFoldDB; Q90303; -.
DR SMR; Q90303; -.
DR Ensembl; ENSCART00000140916; ENSCARP00000124949; ENSCARG00000065561.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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; PS51842; IF_ROD_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT CHAIN 1..467
FT /note="Keratin, type I cytoskeletal 50 kDa"
FT /id="PRO_0000063708"
FT DOMAIN 116..427
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..115
FT /note="Head"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..151
FT /note="Coil 1A"
FT REGION 152..169
FT /note="Linker 1"
FT REGION 170..261
FT /note="Coil 1B"
FT REGION 262..284
FT /note="Linker 12"
FT REGION 285..423
FT /note="Coil 2"
FT REGION 424..467
FT /note="Tail"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 365
FT /note="Stutter"
SQ SEQUENCE 467 AA; 49760 MW; 045647E40160D105 CRC64;
MTSFSRQSFM SSGGGIGGSS MRGPSMGSMS RSSGIGGGGG GHISAMRAGS VYGGAGGHGV
RISTGTRTFA SGGGGGGGAS YGFGGGSGGG GGFGYGSGAG GGFGGGDMDA KVNVSEKATM
QNLNDRLATY LEKVHSLEKA NGDLELKIRQ FLENKTSPDA RDYSAYHATI SDLQDMIQDA
TRINGGVYLA IDNAKLATDD FKTKYENELA MRQSVEADIA GLKRLLDELT LARSDLEMQI
EGLKEELIYL KKNHEEELAS MRSQMTGTVN VEVDAAPQED LSRVMAEIRE QYEGVSAKNQ
RELDAWFQTK SETLTKEVTA NTETLQVSKT EVTELRRTLQ GLEIELQSEL SKKRSLEGTL
ADTESRYSIQ LTQLQARVTS LEEQIVHLRG DMDRQSQEYQ MLLDIKTRLE MEIAEYRRLL
DGGATSFSTS GGGGGGGGGV VSSTKTITVK TIEEDIVDGK VVSSTTK