ID L5JRZ0_PTEAL Unreviewed; 335 AA.
AC L5JRZ0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Keratin-associated protein {ECO:0000256|RuleBase:RU369044};
GN ORFNames=PAL_GLEAN10019572 {ECO:0000313|EMBL:ELK01526.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK01526.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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|RuleBase:RU369044}.
CC -!- SUBUNIT: Interacts with hair keratins. {ECO:0000256|RuleBase:RU369044}.
CC -!- SIMILARITY: Belongs to the PMG family. {ECO:0000256|ARBA:ARBA00034495,
CC ECO:0000256|RuleBase:RU369044}.
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DR EMBL; KB031150; ELK01526.1; -; Genomic_DNA.
DR RefSeq; XP_006925170.1; XM_006925108.1.
DR AlphaFoldDB; L5JRZ0; -.
DR STRING; 9402.L5JRZ0; -.
DR GeneID; 102879051; -.
DR KEGG; pale:102879051; -.
DR CTD; 100533177; -.
DR eggNOG; ENOG502RPU0; Eukaryota.
DR InParanoid; L5JRZ0; -.
DR OrthoDB; 4635903at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0045095; C:keratin filament; IEA:UniProtKB-UniRule.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR InterPro; IPR002494; KAP.
DR InterPro; IPR007659; Keratin_matx.
DR InterPro; IPR007951; KRTAP_PMG.
DR PANTHER; PTHR23260; KERATIN ASSOCIATED PROTEIN 3-3-RELATED; 1.
DR PANTHER; PTHR23260:SF7; KERATIN-ASSOCIATED PROTEIN 26-1; 1.
DR Pfam; PF13885; Keratin_B2_2; 3.
DR Pfam; PF05287; PMG; 1.
PE 3: Inferred from homology;
KW Keratin {ECO:0000256|ARBA:ARBA00022744, ECO:0000256|RuleBase:RU369044};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552}.
SQ SEQUENCE 335 AA; 34341 MW; B29267BFCFC8AD97 CRC64;
MVDSCCPGNA TDIPAVPTIS ICTNRGNFRN GICLPSSCRS RTWQLVTCQE NCQPSSSAPS
GCEPAPCQPT CFPATPCVGF VCQPISSCTA YYKSSTGQPA YLVSSCQPPC SESTGGQPKF
CEASSCQEPV FASGSCQAAC GQSVCCDTGS CQPSCSEVTS HLETSCPSTV CAASPCQPPC
CQAGSCQPAS GENQPCKSTY YQPVCYIFKT CQSVPYTSVP CHPSTCMLSP CSPTCCVSSP
CQPLPCQPAP SISFICQPVA NCQPSCSVKS SCTPASCGTM LSGQPTCVGP TSCNRSSCKS
PSCQPACCVT GLGKSSSGGS NCFQPTPPHL CEAST
//
