ID   A0A452RTJ0_URSAM        Unreviewed;       385 AA.
AC   A0A452RTJ0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Keratin associated protein 16-1 {ECO:0000313|Ensembl:ENSUAMP00000022740.1};
GN   Name=KRTAP16-1 {ECO:0000313|Ensembl:ENSUAMP00000022740.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000022740.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000022740.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: In the hair cortex, hair 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 hair shaft through their extensive disulfide bond
CC       cross-linking with abundant cysteine residues of hair keratins. The
CC       matrix proteins include the high-sulfur and high-glycine-tyrosine
CC       keratins. {ECO:0000256|ARBA:ARBA00003327}.
CC   -!- SUBUNIT: Interacts with hair keratins. {ECO:0000256|ARBA:ARBA00011662}.
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   AlphaFoldDB; A0A452RTJ0; -.
DR   Ensembl; ENSUAMT00000025409.1; ENSUAMP00000022740.1; ENSUAMG00000017840.1.
DR   GeneTree; ENSGT00940000163658; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   InterPro; IPR002494; KAP.
DR   PANTHER; PTHR23262; KERATIN ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR23262:SF55; KERATIN-ASSOCIATED PROTEIN 16-1; 1.
DR   Pfam; PF13885; Keratin_B2_2; 2.
PE   4: Predicted;
KW   Keratin {ECO:0000256|ARBA:ARBA00022744};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022}.
FT   REGION          331..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   385 AA;  40363 MW;  F8123363EEC70A20 CRC64;
     SKMTCCISLC STEVSCGGPV CFSCAQPVCC EATICEPSCA VSSCAQPLCC EATICEPSCA
     VSSCAQPLCC EATICEPSCA VSTCAQPVCC EATICEPSCA VSSCAQPLCL VCEPTCGQPV
     CPTPSCCPSP SCSESSNCQP ASCVALVCEP VCLRPVCCIP SPCEPPCVSS TCQEPSCCIS
     SICQPICSER SPCSASICVP SPCQPTCYVV KRCRSSCREP VSCPSTSCQP LCCRPGSSAS
     AICQPTCSRT FYIPSSCKQP CTPSVSYRPI YRPIFSGPIT YRQPYVTSIS YRPACYRPCY
     SILRRPACVT SLSYRPICSR LPCVDPCRRD CKKSTSSQPD CTDSTSCKAE VSNASPCQTS
     EAKPTSPTTR EAAASPPTAT KPADH
//