ID   KRA31_CAPHI             Reviewed;          98 AA.
AC   P02447; Q6R641;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Keratin-associated protein 3-1;
DE   AltName: Full=Keratin, high sulfur matrix protein, IIIB2;
DE   AltName: Full=Keratin-associated protein 3.2;
DE   AltName: Full=M1.2 protein;
GN   Name=KRTAP3-1;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yin J., Li J.Q., Zhou H.M.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-98, AND ACETYLATION AT ALA-2.
RC   STRAIN=South African angora;
RX   PubMed=1098656; DOI=10.1042/bj1450459;
RA   Parris D., Swart L.S.;
RT   "Studies on the high-sulphur proteins of reduced mohair. The isolation and
RT   amino acid sequence of protein scmkb-m1.2.";
RL   Biochem. J. 145:459-467(1975).
CC   -!- FUNCTION: In the wool cortex, wool keratin intermediate filaments are
CC       embedded in an interfilamentous matrix, consisting of hair keratin-
CC       associated proteins (KRTAP), which are essential for the formation of a
CC       rigid and resistant wool shaft through their extensive disulfide bond
CC       cross-linking with abundant cysteine residues of wool keratins. The
CC       matrix proteins include the high-sulfur and high-glycine-tyrosine
CC       keratins.
CC   -!- SUBUNIT: Interacts with wool keratins.
CC   -!- TISSUE SPECIFICITY: Wool.
CC   -!- SIMILARITY: Belongs to the KRTAP type 3 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY510120; AAS00527.1; -; mRNA.
DR   PIR; A02845; KRGTHM.
DR   RefSeq; NP_001272703.1; NM_001285774.1.
DR   AlphaFoldDB; P02447; -.
DR   STRING; 9925.ENSCHIP00000001041; -.
DR   iPTMnet; P02447; -.
DR   GeneID; 100861180; -.
DR   KEGG; chx:100861180; -.
DR   CTD; 83896; -.
DR   OrthoDB; 1591683at2759; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR007659; Keratin_matx.
DR   PANTHER; PTHR23260; PTHR23260; 1.
DR   Pfam; PF04579; Keratin_matx; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Keratin; Reference proteome;
KW   Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1098656"
FT   CHAIN           2..98
FT                   /note="Keratin-associated protein 3-1"
FT                   /id="PRO_0000185164"
FT   REPEAT          3..7
FT                   /note="1"
FT   REPEAT          8..12
FT                   /note="2"
FT   REPEAT          47..51
FT                   /note="3"
FT   REPEAT          55..59
FT                   /note="4"
FT   REGION          3..59
FT                   /note="4 X 5 AA repeats of C-C-X(3)"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:1098656"
FT   CONFLICT        24
FT                   /note="Q -> K (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   98 AA;  10471 MW;  7AF7F7C4FE35242F CRC64;
     MACCAPRCCS VRTGPATTIC SSDQFCRCGV CLPSTCPHDI SLLQPTFCDN SPVPYHVPDT
     YVPTCFLLNS SHPTPGLSGI NLTTFIQPGC ENACEPRC