ID   K1M1_SHEEP              Reviewed;         412 AA.
AC   P02534; P02536;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 2.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Keratin, type I microfibrillar 48 kDa, component 8C-1;
DE   AltName: Full=Low-sulfur keratin;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX   PubMed=2431679; DOI=10.1042/bj2360695;
RA   Dowling L.M., Crewther W.G., Inglis A.S.;
RT   "The primary structure of component 8c-1, a subunit protein of intermediate
RT   filaments in wool keratin. Relationships with proteins from other
RT   intermediate filaments.";
RL   Biochem. J. 236:695-703(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 133-412.
RX   PubMed=2468578; DOI=10.1016/0378-1119(88)90309-5;
RA   Wilson B.W., Edwards K.J., Sleigh M.J., Byrne C.R., Ward K.A.;
RT   "Complete sequence of a type-I microfibrillar wool keratin gene.";
RL   Gene 73:21-31(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 220-366.
RX   PubMed=6188504; DOI=10.1007/bf01121573;
RA   Dowling L.M., Parry D.A.D., Sparrow L.G.;
RT   "Structural homology between hard alpha-keratin and the intermediate
RT   filament proteins desmin and vimentin.";
RL   Biosci. Rep. 3:73-78(1983).
CC   -!- FUNCTION: Wool microfibrillar keratin.
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   -!- MISCELLANEOUS: The low-sulfur proteins, derived from the microfibrillar
CC       fraction of wool extracts, are composed of two families, each
CC       consisting of 4 homologous subunits: the type I components (8C-1, 8C-2,
CC       8A and 8B) and the type II components (5, 7A, 7B, and 7C).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; M23913; AAA31556.1; -; mRNA.
DR   PIR; A02942; KRSHL1.
DR   PIR; S07158; S07158.
DR   AlphaFoldDB; P02534; -.
DR   SMR; P02534; -.
DR   iPTMnet; P02534; -.
DR   PRIDE; P02534; -.
DR   eggNOG; ENOG502SNBF; Eukaryota.
DR   Proteomes; UP000002356; 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   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Direct protein sequencing; Intermediate filament;
KW   Keratin; Reference proteome.
FT   CHAIN           1..412
FT                   /note="Keratin, type I microfibrillar 48 kDa, component 8C-
FT                   1"
FT                   /id="PRO_0000063706"
FT   DOMAIN          55..366
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..55
FT                   /note="Head"
FT   REGION          56..90
FT                   /note="Coil 1A"
FT   REGION          91..101
FT                   /note="Linker 1"
FT   REGION          102..202
FT                   /note="Coil 1B"
FT   REGION          203..218
FT                   /note="Linker 12"
FT   REGION          219..362
FT                   /note="Coil 2"
FT   REGION          363..412
FT                   /note="Tail"
FT   SITE            304
FT                   /note="Stutter"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2431679"
FT   CONFLICT        159
FT                   /note="N -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        266..269
FT                   /note="SCQT -> CNQE (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="E -> Q (in Ref. 1; AA sequence and 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   412 AA;  46674 MW;  8C927460832741E0 CRC64;
     SFNFCLPNLS FRSSCSSRPC VPSSCCGTTL PGACNIPANV GSCNWFCEGS FDGNEKETMQ
     FLNDRLASYL EKVRQLEREN AELESRILER SQQQEPLVCP NYQSYFRTIE ELQQKILCAK
     SENARLVVQI DNAKLAADDF RTKYETELGL RQLVESDING LRRILDELTL CKSDLEAQVE
     SLKEELICLK SNHEEEVNTL RSQLGDRLNV EVDAAPTVDL NRVLNETRAQ YEALVETNRR
     DVEEWYIRQT EELNKQVVSS SEQLQSCQTE IIELRRTVNA LEVELQAQHN LRDSLENTLT
     ETEARYSCQL NQVQSLISNV ESQLAEIRGD LERQNQEYQV LLDVRARLEC EINTYRGLLD
     SEDCKLPCNP CATTNACGKT ITPCISSPCA PAAPCTPCVP RSRCGPCNSY VR