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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
 
 
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