ID G1QG38_MYOLU Unreviewed; 216 AA.
AC G1QG38;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000022671.1};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000022671.1, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000022671.1, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000022671.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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DR EMBL; AAPE02029688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QG38; -.
DR Ensembl; ENSMLUT00000007797.2; ENSMLUP00000022671.1; ENSMLUG00000010189.2.
DR GeneTree; ENSGT00940000163931; -.
DR Proteomes; UP000001074; 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:SF183; KERATIN-ASSOCIATED PROTEIN 4-11-RELATED; 1.
DR Pfam; PF13885; Keratin_B2_2; 2.
PE 4: Predicted;
KW Keratin {ECO:0000256|ARBA:ARBA00022744};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074}.
SQ SEQUENCE 216 AA; 21989 MW; 93F9E6C5C2125E7E CRC64;
MVNSCCGSVC SDQGCGQGCC QETCCRPSCC QTTCCRPSCC QTTCCRPSCC VSSCCRPSCC
CCQTSCCRPS CCISSCCRPS CCGSSCCGSS CCRPSCCISS CCRPSCCGSS CCGSSCCRPS
CCISSCCRPS CCGSSCCGSS CCRPSCCISS CCRPSCCGSS CCGSSCCGSS CCRPSCCPCC
CLRPVCGQVS CCTNCYRPTC VISTCPRPMC CAIPDC
//
