CHID1_HUMAN
ID CHID1_HUMAN Reviewed; 393 AA.
AC Q9BWS9; B3KWB0; Q8NBM9; Q96CZ3; Q96S93; Q96SK0; Q9BY52;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Chitinase domain-containing protein 1;
DE AltName: Full=Stabilin-1-interacting chitinase-like protein;
DE Short=SI-CLP;
DE Flags: Precursor;
GN Name=CHID1; ORFNames=GL008, PSEC0104, SB139;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH STAB1, AND TISSUE SPECIFICITY.
RX PubMed=16357325; DOI=10.1182/blood-2005-07-2843;
RA Kzhyshkowska J., Mamidi S., Gratchev A., Kremmer E., Schmuttermaier C.,
RA Krusell L., Haus G., Utikal J., Schledzewski K., Scholtze J., Goerdt S.;
RT "Novel stabilin-1 interacting chitinase-like protein (SI-CLP) is up-
RT regulated in alternatively activated macrophages and secreted via lysosomal
RT pathway.";
RL Blood 107:3221-3228(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-338.
RC TISSUE=Liver;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human liver non-tumor tissues.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Li N., Wan T., Zhang W., Cao X.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-338.
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLN-331
RP AND VAL-338.
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), TISSUE SPECIFICITY, INDUCTION,
RP MUTAGENESIS OF TYR-84; TRP-88; TRP-110; TYR-261; TRP-277 AND TYR-302, AND
RP FUNCTION.
RX PubMed=20724479; DOI=10.1074/jbc.m110.130781;
RA Meng G., Zhao Y., Bai X., Liu Y., Green T.J., Luo M., Zheng X.;
RT "Structure of human stabilin-1 interacting chitinase-like protein (SI-CLP)
RT reveals a saccharide-binding cleft with lower sugar-binding selectivity.";
RL J. Biol. Chem. 285:39898-39904(2010).
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). {ECO:0000269|PubMed:20724479}.
CC -!- SUBUNIT: Interacts with STAB1. {ECO:0000269|PubMed:16357325}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16357325}. Lysosome
CC {ECO:0000269|PubMed:16357325}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BWS9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWS9-2; Sequence=VSP_023825;
CC Name=3;
CC IsoId=Q9BWS9-3; Sequence=VSP_023826;
CC -!- TISSUE SPECIFICITY: Expressed in cells of monocytic, T, B and
CC epithelial origin. {ECO:0000269|PubMed:16357325,
CC ECO:0000269|PubMed:20724479}.
CC -!- INDUCTION: Up-regulated by IL4/interleukin-4 and dexamethasone in the
CC macrophages. Up-regulated by glucocorticoid.
CC {ECO:0000269|PubMed:16357325, ECO:0000269|PubMed:20724479}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 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; BN000479; CAF32458.1; -; mRNA.
DR EMBL; AF212229; AAK14915.1; -; mRNA.
DR EMBL; AY037151; AAK67632.1; -; mRNA.
DR EMBL; AK027711; BAB55316.1; -; mRNA.
DR EMBL; AK075413; BAC11603.1; -; mRNA.
DR EMBL; AK124697; BAG54072.1; -; mRNA.
DR EMBL; BC000001; AAH00001.1; -; mRNA.
DR EMBL; BC013642; AAH13642.1; -; mRNA.
DR EMBL; BC095409; AAH95409.1; -; mRNA.
DR CCDS; CCDS44510.1; -. [Q9BWS9-3]
DR CCDS; CCDS44511.1; -. [Q9BWS9-2]
DR CCDS; CCDS7722.1; -. [Q9BWS9-1]
DR RefSeq; NP_001136146.1; NM_001142674.1. [Q9BWS9-1]
DR RefSeq; NP_001136147.1; NM_001142675.1. [Q9BWS9-1]
DR RefSeq; NP_001136148.1; NM_001142676.1. [Q9BWS9-2]
DR RefSeq; NP_001136149.1; NM_001142677.1. [Q9BWS9-3]
DR RefSeq; NP_076436.3; NM_023947.3. [Q9BWS9-1]
DR RefSeq; XP_005253130.1; XM_005253073.4. [Q9BWS9-3]
DR RefSeq; XP_006718345.1; XM_006718282.2. [Q9BWS9-1]
DR RefSeq; XP_016873655.1; XM_017018166.1. [Q9BWS9-1]
DR PDB; 3BXW; X-ray; 2.70 A; A/B=1-393.
DR PDBsum; 3BXW; -.
DR AlphaFoldDB; Q9BWS9; -.
DR SMR; Q9BWS9; -.
DR BioGRID; 122451; 80.
DR IntAct; Q9BWS9; 1.
DR STRING; 9606.ENSP00000398722; -.
DR UniLectin; Q9BWS9; -.
DR iPTMnet; Q9BWS9; -.
DR PhosphoSitePlus; Q9BWS9; -.
DR BioMuta; CHID1; -.
DR DMDM; 74733460; -.
DR EPD; Q9BWS9; -.
DR jPOST; Q9BWS9; -.
DR MassIVE; Q9BWS9; -.
DR MaxQB; Q9BWS9; -.
DR PeptideAtlas; Q9BWS9; -.
DR PRIDE; Q9BWS9; -.
DR ProteomicsDB; 79306; -. [Q9BWS9-1]
DR ProteomicsDB; 79307; -. [Q9BWS9-2]
DR ProteomicsDB; 79308; -. [Q9BWS9-3]
DR TopDownProteomics; Q9BWS9-2; -. [Q9BWS9-2]
DR Antibodypedia; 10139; 210 antibodies from 24 providers.
DR DNASU; 66005; -.
DR Ensembl; ENST00000323578.13; ENSP00000325055.8; ENSG00000177830.18. [Q9BWS9-1]
DR Ensembl; ENST00000429789.6; ENSP00000416034.2; ENSG00000177830.18. [Q9BWS9-3]
DR Ensembl; ENST00000436108.6; ENSP00000388156.2; ENSG00000177830.18. [Q9BWS9-1]
DR Ensembl; ENST00000449825.5; ENSP00000391255.1; ENSG00000177830.18. [Q9BWS9-1]
DR Ensembl; ENST00000454838.6; ENSP00000398722.2; ENSG00000177830.18. [Q9BWS9-2]
DR Ensembl; ENST00000528581.5; ENSP00000435503.1; ENSG00000177830.18. [Q9BWS9-2]
DR GeneID; 66005; -.
DR KEGG; hsa:66005; -.
DR MANE-Select; ENST00000323578.13; ENSP00000325055.8; NM_023947.4; NP_076436.3.
DR UCSC; uc001lsm.4; human. [Q9BWS9-1]
DR CTD; 66005; -.
DR DisGeNET; 66005; -.
DR GeneCards; CHID1; -.
DR HGNC; HGNC:28474; CHID1.
DR HPA; ENSG00000177830; Low tissue specificity.
DR MIM; 615692; gene.
DR neXtProt; NX_Q9BWS9; -.
DR OpenTargets; ENSG00000177830; -.
DR PharmGKB; PA142672118; -.
DR VEuPathDB; HostDB:ENSG00000177830; -.
DR eggNOG; KOG2091; Eukaryota.
DR GeneTree; ENSGT00390000012069; -.
DR HOGENOM; CLU_035132_2_0_1; -.
DR InParanoid; Q9BWS9; -.
DR OMA; YSINERI; -.
DR OrthoDB; 1067925at2759; -.
DR PhylomeDB; Q9BWS9; -.
DR TreeFam; TF319271; -.
DR PathwayCommons; Q9BWS9; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q9BWS9; -.
DR BioGRID-ORCS; 66005; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; CHID1; human.
DR EvolutionaryTrace; Q9BWS9; -.
DR GenomeRNAi; 66005; -.
DR Pharos; Q9BWS9; Tbio.
DR PRO; PR:Q9BWS9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BWS9; protein.
DR Bgee; ENSG00000177830; Expressed in stromal cell of endometrium and 180 other tissues.
DR ExpressionAtlas; Q9BWS9; baseline and differential.
DR Genevisible; Q9BWS9; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0070492; F:oligosaccharide binding; IPI:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
DR Gene3D; 3.10.50.10; -; 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 Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Immunity; Innate immunity; Lysosome;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..393
FT /note="Chitinase domain-containing protein 1"
FT /id="PRO_0000280608"
FT DOMAIN 79..393
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT VAR_SEQ 37
FT /note="K -> KVKFCSCCPGWSAMARSWLTATSATQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743"
FT /id="VSP_023825"
FT VAR_SEQ 204..234
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_023826"
FT VARIANT 331
FT /note="R -> Q (in dbSNP:rs1127800)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031173"
FT VARIANT 338
FT /note="A -> V (in dbSNP:rs6682)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_031174"
FT MUTAGEN 84
FT /note="Y->S: Significantly decreased carbohydrate binding."
FT /evidence="ECO:0000269|PubMed:20724479"
FT MUTAGEN 88
FT /note="W->A: Significantly decreased carbohydrate binding."
FT /evidence="ECO:0000269|PubMed:20724479"
FT MUTAGEN 110
FT /note="W->A: Significantly decreased carbohydrate binding."
FT /evidence="ECO:0000269|PubMed:20724479"
FT MUTAGEN 261
FT /note="Y->S: Significantly decreased carbohydrate binding."
FT /evidence="ECO:0000269|PubMed:20724479"
FT MUTAGEN 277
FT /note="W->A: No noticeable effect."
FT /evidence="ECO:0000269|PubMed:20724479"
FT MUTAGEN 302
FT /note="Y->S: Significantly decreased carbohydrate binding."
FT /evidence="ECO:0000269|PubMed:20724479"
FT CONFLICT 335
FT /note="D -> G (in Ref. 4; BAB55316)"
FT /evidence="ECO:0000305"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:3BXW"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 167..184
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 202..218
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:3BXW"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 243..249
FT /evidence="ECO:0007829|PDB:3BXW"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 295..307
FT /evidence="ECO:0007829|PDB:3BXW"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:3BXW"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:3BXW"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:3BXW"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:3BXW"
FT HELIX 387..392
FT /evidence="ECO:0007829|PDB:3BXW"
SQ SEQUENCE 393 AA; 44941 MW; FFD5E67C20AF69B4 CRC64;
MRTLFNLLWL ALACSPVHTT LSKSDAKKAA SKTLLEKSQF SDKPVQDRGL VVTDLKAESV
VLEHRSYCSA KARDRHFAGD VLGYVTPWNS HGYDVTKVFG SKFTQISPVW LQLKRRGREM
FEVTGLHDVD QGWMRAVRKH AKGLHIVPRL LFEDWTYDDF RNVLDSEDEI EELSKTVVQV
AKNQHFDGFV VEVWNQLLSQ KRVGLIHMLT HLAEALHQAR LLALLVIPPA ITPGTDQLGM
FTHKEFEQLA PVLDGFSLMT YDYSTAHQPG PNAPLSWVRA CVQVLDPKSK WRSKILLGLN
FYGMDYATSK DAREPVVGAR YIQTLKDHRP RMVWDSQASE HFFEYKKSRS GRHVVFYPTL
KSLQVRLELA RELGVGVSIW ELGQGLDYFY DLL
