ID   K2M3_SHEEP              Reviewed;         502 AA.
AC   P25691;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Keratin, type II microfibrillar, component 5;
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.
RC   STRAIN=Merino; TISSUE=Wool;
RX   PubMed=1371668; DOI=10.1042/bj2820291;
RA   Sparrow L.G., Robinson C.P., Caine J., McMahon D.T.W., Strike P.M.;
RT   "Type II intermediate-filament proteins from wool. The amino acid sequence
RT   of component 5 and comparison with component 7c.";
RL   Biochem. J. 282:291-297(1992).
CC   -!- FUNCTION: Wool microfibrillar keratin.
CC   -!- TISSUE SPECIFICITY: Hard keratin wool.
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   PIR; S29094; S29094.
DR   AlphaFoldDB; P25691; -.
DR   SMR; P25691; -.
DR   STRING; 9940.ENSOARP00000018352; -.
DR   PRIDE; P25691; -.
DR   eggNOG; ENOG502SK5S; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF16208; Keratin_2_head; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
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   Coiled coil; Direct protein sequencing; Intermediate filament;
KW   Isopeptide bond; Keratin; Reference proteome; Ubl conjugation.
FT   CHAIN           1..502
FT                   /note="Keratin, type II microfibrillar, component 5"
FT                   /id="PRO_0000063749"
FT   DOMAIN          122..433
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..122
FT                   /note="Head"
FT   REGION          123..157
FT                   /note="Coil 1A"
FT   REGION          158..167
FT                   /note="Linker 1"
FT   REGION          168..268
FT                   /note="Coil 1B"
FT   REGION          269..285
FT                   /note="Linker 12"
FT   REGION          286..429
FT                   /note="Coil 2"
FT   REGION          430..502
FT                   /note="Tail"
FT   MOD_RES         1
FT                   /note="Blocked amino end (Ser)"
FT   CROSSLNK        228
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P78386"
FT   UNSURE          1..2
FT                   /note="SC or CS"
SQ   SEQUENCE   502 AA;  55255 MW;  8734C8230550CE68 CRC64;
     SCRSYRISPG YSVTRTFSSC SAVAPKTGSR CCISAAPYRG VSCYRGLTGF GSRSVSALGS
     CGPRIAVSGF RAGSCGRSFG YRSGGVGGLS PSCITTVSVN ESLLTPLNLE IDPNAQCVKH
     QEKEQIKNLN SRFAAFIDKV RFLEQQNKLL ETKWQFYQNQ RCCESNLEPL FNGYIETLRR
     EAEHVEADSG RLASELDHVQ EVLEGYKKKY EEEVALRATA ENEFVVLKKD VDCAYLRKSD
     LEANVEALVE ESNFLKRLYD EEIQILNAHI SDTSVIVKMD NSRDLNMDCV VAEIKAQYDD
     IASRSRAEAE SWYRSKCEEM KATVIRHGET LRRTKEEINE LNRVIQRLTA EIENAKCQRT
     KLEAAVAEAE QQGEAALNDA RSKLAGLEEA LQKAKQDMAC LLKEYQEVMN SKLGLDIEIA
     TYRRLLEGEE QRLCEGVGSV NVCVSSRGGV ACGGLTYSST AGRQIASGPV ATGGSITVLA
     PDSCQPRASS FSCGSSRSVR FA