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Database: UniProt
Entry: A0A2K5VN88_MACFA
LinkDB: A0A2K5VN88_MACFA
Original site: A0A2K5VN88_MACFA 
ID   A0A2K5VN88_MACFA        Unreviewed;       418 AA.
AC   A0A2K5VN88;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Chitinase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00040976};
GN   Name=CHID1 {ECO:0000313|Ensembl:ENSMFAP00000026246.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000026246.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000026246.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000026246.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Saccharide- and LPS-binding protein with possible roles in
CC       pathogen sensing and endotoxin neutralization. Ligand-binding
CC       specificity relates to the length of the oligosaccharides, with
CC       preference for chitotetraose (in vitro).
CC       {ECO:0000256|ARBA:ARBA00037756}.
CC   -!- SUBUNIT: Interacts with STAB1. {ECO:0000256|ARBA:ARBA00038832}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|ARBA:ARBA00009336}.
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DR   AlphaFoldDB; A0A2K5VN88; -.
DR   STRING; 9541.ENSMFAP00000026246; -.
DR   Ensembl; ENSMFAT00000029745.2; ENSMFAP00000026246.2; ENSMFAG00000044543.2.
DR   VEuPathDB; HostDB:ENSMFAG00000044543; -.
DR   GeneTree; ENSGT00390000012069; -.
DR   Proteomes; UP000233100; Chromosome 14.
DR   Bgee; ENSMFAG00000044543; Expressed in pituitary gland and 13 other cell types or tissues.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02876; GH18_SI-CLP; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 1.10.8.360; 3,6-anhydro-alpha-l-galactosidase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR029070; Chitinase_insertion_sf.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR46066:SF2; CHITINASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR46066; CHITINASE DOMAIN-CONTAINING PROTEIN 1 FAMILY MEMBER; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..418
FT                   /note="Chitinase domain-containing protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5030051651"
FT   DOMAIN          104..418
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   418 AA;  47660 MW;  19A748DB10C1DBC6 CRC64;
     MRTLFNILWL ALACSPVHTT LSKSDAKKAA SKTLLEKMKF RSCCPGWSAV ARSWLTATSA
     TQSQFSDKPV QDRGLVVTDL KAESVVLEHR SYCSAKARDR HFAGDVLGYV TPWNSHGYDV
     TKVFGSKFTQ ISPVWLQLKR RGREMFEVTG LHDVDQGWMR AIRKNAKGLH IVPRLLFEDW
     TYDDFRNVLD SEDEIEELSK TVVQVAKNQH FDGFVVEVWN QLLSQKRVGL IHMLTHLAEA
     LHQARLLALL VIPPAITPGT DQLGMFTHKE FEQLAPVLDG FSLMTYDYST AHQPGPNAPL
     SWVRACVQVL DPKSKWRSKI LLGLNFYGMD YATSKDAREP VVGARYIQTL KDHRPRMVWD
     SQASEHFFEY KKSRSGRHVV FYPTLKSLQV RLELARELGV GVSIWELGQG LDYFYDLL
//
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