HYAL1_HUMAN
ID HYAL1_HUMAN Reviewed; 435 AA.
AC Q12794; Q6FH23; Q6PIZ6; Q7KYU2; Q7LE34; Q8NFK5; Q8NFK6; Q8NFK7; Q8NFK8;
AC Q8NFK9; Q93013; Q9UKD5; Q9UNI8;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Hyaluronidase-1;
DE Short=Hyal-1;
DE EC=3.2.1.35;
DE AltName: Full=Hyaluronoglucosaminidase-1;
DE AltName: Full=Lung carcinoma protein 1;
DE Short=LuCa-1;
DE Flags: Precursor;
GN Name=HYAL1; Synonyms=LUCA1;
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).
RC TISSUE=Heart, and Lung cancer;
RX PubMed=8603390;
RA Wei M.H., Latif F., Bader S., Kashuba V., Chen J.Y., Duh F.-M., Sekido Y.,
RA Lee C.C., Geil L., Kuzmin I., Zabarovsky E., Klein G., Zbar B., Minna J.D.,
RA Lerman M.I.;
RT "Construction of a 600-kilobase cosmid clone contig and generation of a
RT transcriptional map surrounding the lung cancer tumor suppressor gene (TSG)
RT locus on human chromosome 3p21.3: progress toward the isolation of a lung
RT cancer TSG.";
RL Cancer Res. 56:1487-1492(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 22-37; 72-84;
RP 248-259 AND 261-273, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Plasma;
RX PubMed=9223416; DOI=10.1006/bbrc.1997.6773;
RA Frost G.I., Csoka A.B., Wong T., Stern R.;
RT "Purification, cloning, and expression of human plasma hyaluronidase.";
RL Biochem. Biophys. Res. Commun. 236:10-15(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10702795; DOI=10.1038/sj.onc.1203317;
RA Frost G.I., Mohapatra G., Wong T.M., Csoka A.B., Gray J.W., Stern R.;
RT "HYAL1(LUCA-1), a candidate tumor suppressor gene on chromosome 3p21.3, is
RT inactivated in head and neck squamous cell carcinomas by aberrant splicing
RT of pre-mRNA.";
RL Oncogene 19:870-877(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), FUNCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12084718; DOI=10.1074/jbc.m203821200;
RA Lokeshwar V.B., Schroeder G.L., Carey R.I., Soloway M.S., Iida N.;
RT "Regulation of hyaluronidase activity by alternative mRNA splicing.";
RL J. Biol. Chem. 277:33654-33663(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Forgacs E., Sekido Y., Bader S., Cundiff S., Compton L., Latif F.,
RA Lerman M.I., Minna J.D.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7).
RC TISSUE=Colon, and Pancreas;
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-435, IDENTIFICATION BY MASS
RP SPECTROMETRY, GLYCOSYLATION AT ASN-99; ASN-216 AND ASN-350, AND DISULFIDE
RP BONDS.
RX PubMed=17503783; DOI=10.1021/bi700382g;
RA Chao K.L., Muthukumar L., Herzberg O.;
RT "Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme
RT involved in tumor growth and angiogenesis.";
RL Biochemistry 46:6911-6920(2007).
RN [10]
RP VARIANT MPS9 LYS-268, AND TISSUE SPECIFICITY.
RX PubMed=10339581; DOI=10.1073/pnas.96.11.6296;
RA Triggs-Raine B., Salo T.J., Zhang H., Wicklow B.A., Natowicz M.R.;
RT "Mutations in HYAL1, a member of a tandemly distributed multigene family
RT encoding disparate hyaluronidase activities, cause a newly described
RT lysosomal disorder, mucopolysaccharidosis IX.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6296-6300(1999).
CC -!- FUNCTION: May have a role in promoting tumor progression. May block the
CC TGFB1-enhanced cell growth. {ECO:0000269|PubMed:12084718}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is about 3.8.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9223416}. Lysosome
CC {ECO:0000269|PubMed:9223416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q12794-1; Sequence=Displayed;
CC Name=2; Synonyms=HYAl1v1;
CC IsoId=Q12794-2; Sequence=VSP_015920;
CC Name=3; Synonyms=HYAl1v2;
CC IsoId=Q12794-3; Sequence=VSP_015917;
CC Name=4; Synonyms=HYAl1v3;
CC IsoId=Q12794-4; Sequence=VSP_015918, VSP_015919;
CC Name=5; Synonyms=HYAl1v4;
CC IsoId=Q12794-5; Sequence=VSP_015916;
CC Name=6; Synonyms=HYAl1v5;
CC IsoId=Q12794-6; Sequence=VSP_015915;
CC Name=7;
CC IsoId=Q12794-7; Sequence=VSP_015921, VSP_015922;
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver, kidney and heart.
CC Weakly expressed in lung, placenta and skeletal muscle. No expression
CC detected in adult brain. Isoform 1 is expressed only in bladder and
CC prostate cancer cells, G2/G3 bladder tumor tissues and lymph node
CC specimens showing tumor invasive tumors cells. Isoform 3, isoform 4,
CC isoform 5 and isoform 6 are expressed in normal bladder and bladder
CC tumor tissues. {ECO:0000269|PubMed:10339581,
CC ECO:0000269|PubMed:12084718, ECO:0000269|PubMed:9223416}.
CC -!- DISEASE: Mucopolysaccharidosis 9 (MPS9) [MIM:601492]: A form of
CC mucopolysaccharidosis, a group of lysosomal storage diseases
CC characterized by defective degradation of glycosaminoglycans, resulting
CC in their excessive accumulation and secretion. The diseases are
CC progressive and often display a wide spectrum of clinical severity.
CC MPS9 is an autosomal recessive form characterized by high hyaluronan
CC concentration in the serum. Clinical features include periarticular
CC soft tissue masses, mild short stature and acetabular erosions, and
CC absence of neurological or visceral involvement.
CC {ECO:0000269|PubMed:10339581}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Enzymatically inactive. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Enzymatically inactive. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Enzymatically inactive. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Enzymatically inactive. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Enzymatically inactive. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25774.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HYAL1ID40903ch3p21.html";
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DR EMBL; U03056; AAD09137.2; -; mRNA.
DR EMBL; U96078; AAD04190.1; -; mRNA.
DR EMBL; AF118821; AAD24460.1; -; mRNA.
DR EMBL; AF502904; AAM60770.1; -; mRNA.
DR EMBL; AF502905; AAM60771.1; -; mRNA.
DR EMBL; AF502906; AAM60772.1; -; mRNA.
DR EMBL; AF502907; AAM60773.1; -; mRNA.
DR EMBL; AF502908; AAM60774.1; -; mRNA.
DR EMBL; AF173154; AAD53277.1; -; mRNA.
DR EMBL; CR541933; CAG46731.1; -; mRNA.
DR EMBL; AC002455; AAB67046.1; -; Genomic_DNA.
DR EMBL; U73167; AAC02730.1; -; Genomic_DNA.
DR EMBL; BC025774; AAH25774.1; ALT_INIT; mRNA.
DR EMBL; BC035695; AAH35695.1; -; mRNA.
DR CCDS; CCDS2816.1; -. [Q12794-1]
DR CCDS; CCDS2817.1; -. [Q12794-2]
DR CCDS; CCDS46832.1; -. [Q12794-3]
DR CCDS; CCDS46833.1; -. [Q12794-5]
DR PIR; JC5584; JC5584.
DR RefSeq; NP_149349.2; NM_033159.3. [Q12794-1]
DR RefSeq; NP_695013.1; NM_153281.1. [Q12794-1]
DR RefSeq; NP_695014.1; NM_153282.2. [Q12794-2]
DR RefSeq; NP_695015.1; NM_153283.2. [Q12794-3]
DR RefSeq; NP_695017.1; NM_153285.2. [Q12794-5]
DR RefSeq; XP_011531969.1; XM_011533667.2. [Q12794-1]
DR RefSeq; XP_011531970.1; XM_011533668.2. [Q12794-1]
DR RefSeq; XP_011531971.1; XM_011533669.2. [Q12794-1]
DR PDB; 2PE4; X-ray; 2.00 A; A=22-435.
DR PDBsum; 2PE4; -.
DR AlphaFoldDB; Q12794; -.
DR SMR; Q12794; -.
DR BioGRID; 109603; 35.
DR IntAct; Q12794; 8.
DR STRING; 9606.ENSP00000266031; -.
DR BindingDB; Q12794; -.
DR ChEMBL; CHEMBL4528; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR CAZy; GH56; Glycoside Hydrolase Family 56.
DR GlyGen; Q12794; 3 sites.
DR iPTMnet; Q12794; -.
DR PhosphoSitePlus; Q12794; -.
DR BioMuta; HYAL1; -.
DR DMDM; 74735617; -.
DR jPOST; Q12794; -.
DR MassIVE; Q12794; -.
DR MaxQB; Q12794; -.
DR PaxDb; Q12794; -.
DR PeptideAtlas; Q12794; -.
DR PRIDE; Q12794; -.
DR ProteomicsDB; 58936; -. [Q12794-1]
DR ProteomicsDB; 58937; -. [Q12794-2]
DR ProteomicsDB; 58938; -. [Q12794-3]
DR ProteomicsDB; 58939; -. [Q12794-4]
DR ProteomicsDB; 58940; -. [Q12794-5]
DR ProteomicsDB; 58941; -. [Q12794-6]
DR ProteomicsDB; 58942; -. [Q12794-7]
DR Antibodypedia; 1046; 291 antibodies from 30 providers.
DR DNASU; 3373; -.
DR Ensembl; ENST00000266031.8; ENSP00000266031.4; ENSG00000114378.17. [Q12794-1]
DR Ensembl; ENST00000320295.12; ENSP00000346068.5; ENSG00000114378.17. [Q12794-1]
DR Ensembl; ENST00000395143.6; ENSP00000378575.2; ENSG00000114378.17. [Q12794-2]
DR Ensembl; ENST00000395144.7; ENSP00000378576.2; ENSG00000114378.17. [Q12794-1]
DR Ensembl; ENST00000447605.2; ENSP00000390149.2; ENSG00000114378.17. [Q12794-5]
DR Ensembl; ENST00000457214.6; ENSP00000393358.2; ENSG00000114378.17. [Q12794-3]
DR Ensembl; ENST00000618175.4; ENSP00000477903.1; ENSG00000114378.17. [Q12794-1]
DR GeneID; 3373; -.
DR KEGG; hsa:3373; -.
DR MANE-Select; ENST00000395144.7; ENSP00000378576.2; NM_033159.4; NP_149349.2.
DR UCSC; uc003czm.5; human. [Q12794-1]
DR CTD; 3373; -.
DR DisGeNET; 3373; -.
DR GeneCards; HYAL1; -.
DR HGNC; HGNC:5320; HYAL1.
DR HPA; ENSG00000114378; Tissue enhanced (liver, lymphoid tissue).
DR MalaCards; HYAL1; -.
DR MIM; 601492; phenotype.
DR MIM; 607071; gene.
DR neXtProt; NX_Q12794; -.
DR OpenTargets; ENSG00000114378; -.
DR Orphanet; 67041; Hyaluronidase deficiency.
DR PharmGKB; PA29571; -.
DR VEuPathDB; HostDB:ENSG00000114378; -.
DR eggNOG; ENOG502QTUU; Eukaryota.
DR GeneTree; ENSGT01020000230364; -.
DR HOGENOM; CLU_036366_0_0_1; -.
DR InParanoid; Q12794; -.
DR OMA; GQCPLGI; -.
DR PhylomeDB; Q12794; -.
DR TreeFam; TF321598; -.
DR BioCyc; MetaCyc:HS03763-MON; -.
DR BRENDA; 3.2.1.35; 2681.
DR BRENDA; 4.2.2.1; 2681.
DR PathwayCommons; Q12794; -.
DR Reactome; R-HSA-2024101; CS/DS degradation.
DR Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-HSA-2206280; MPS IX - Natowicz syndrome.
DR SignaLink; Q12794; -.
DR SIGNOR; Q12794; -.
DR BioGRID-ORCS; 3373; 7 hits in 1076 CRISPR screens.
DR EvolutionaryTrace; Q12794; -.
DR GeneWiki; HYAL1; -.
DR GenomeRNAi; 3373; -.
DR Pharos; Q12794; Tbio.
DR PRO; PR:Q12794; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q12794; protein.
DR Bgee; ENSG00000114378; Expressed in right lobe of liver and 101 other tissues.
DR ExpressionAtlas; Q12794; baseline and differential.
DR Genevisible; Q12794; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0036117; C:hyaluranon cable; IDA:UniProtKB.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0050501; F:hyaluronan synthase activity; IDA:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0051216; P:cartilage development; IEP:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
DR GO; GO:0071467; P:cellular response to pH; IDA:UniProtKB.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:UniProtKB.
DR GO; GO:0071493; P:cellular response to UV-B; IDA:UniProtKB.
DR GO; GO:0030207; P:chondroitin sulfate catabolic process; TAS:Reactome.
DR GO; GO:0060272; P:embryonic skeletal joint morphogenesis; IEA:Ensembl.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
DR GO; GO:0030212; P:hyaluronan metabolic process; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IDA:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0045927; P:positive regulation of growth; IDA:UniProtKB.
DR GO; GO:1900106; P:positive regulation of hyaluranon cable assembly; IDA:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR GO; GO:0000302; P:response to reactive oxygen species; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR PANTHER; PTHR11769; PTHR11769; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01186; EGF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disease variant; Disulfide bond; EGF-like domain; Glycoprotein;
KW Glycosidase; Hydrolase; Lysosome; Mucopolysaccharidosis;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..435
FT /note="Hyaluronidase-1"
FT /id="PRO_0000042622"
FT DOMAIN 354..430
FT /note="EGF-like"
FT ACT_SITE 131
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17503783"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17503783"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17503783"
FT DISULFID 43..333
FT /evidence="ECO:0000269|PubMed:17503783"
FT DISULFID 207..221
FT /evidence="ECO:0000269|PubMed:17503783"
FT DISULFID 358..369
FT /evidence="ECO:0000269|PubMed:17503783"
FT DISULFID 363..418
FT /evidence="ECO:0000269|PubMed:17503783"
FT DISULFID 420..429
FT /evidence="ECO:0000269|PubMed:17503783"
FT VAR_SEQ 1..339
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12084718"
FT /id="VSP_015915"
FT VAR_SEQ 1..259
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12084718"
FT /id="VSP_015916"
FT VAR_SEQ 1..182
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12084718"
FT /id="VSP_015917"
FT VAR_SEQ 208..209
FT /note="YN -> SG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12084718"
FT /id="VSP_015918"
FT VAR_SEQ 210..435
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12084718"
FT /id="VSP_015919"
FT VAR_SEQ 301..330
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12084718, ECO:0000303|Ref.6"
FT /id="VSP_015920"
FT VAR_SEQ 331..336
FT /note="ESCQAI -> VSLGLA (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015921"
FT VAR_SEQ 337..435
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015922"
FT VARIANT 268
FT /note="E -> K (in MPS9; dbSNP:rs104893743)"
FT /evidence="ECO:0000269|PubMed:10339581"
FT /id="VAR_023643"
FT CONFLICT 3
FT /note="A -> G (in Ref. 6; CAG46731)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="R -> G (in Ref. 1; AAD53277)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="L -> Q (in Ref. 3; AAD24460)"
FT /evidence="ECO:0000305"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 164..193
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 258..275
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 344..362
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:2PE4"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:2PE4"
FT HELIX 406..415
FT /evidence="ECO:0007829|PDB:2PE4"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:2PE4"
FT TURN 426..429
FT /evidence="ECO:0007829|PDB:2PE4"
SQ SEQUENCE 435 AA; 48368 MW; 9C2B2D8DB361E0BB CRC64;
MAAHLLPICA LFLTLLDMAQ GFRGPLLPNR PFTTVWNANT QWCLERHGVD VDVSVFDVVA
NPGQTFRGPD MTIFYSSQLG TYPYYTPTGE PVFGGLPQNA SLIAHLARTF QDILAAIPAP
DFSGLAVIDW EAWRPRWAFN WDTKDIYRQR SRALVQAQHP DWPAPQVEAV AQDQFQGAAR
AWMAGTLQLG RALRPRGLWG FYGFPDCYNY DFLSPNYTGQ CPSGIRAQND QLGWLWGQSR
ALYPSIYMPA VLEGTGKSQM YVQHRVAEAF RVAVAAGDPN LPVLPYVQIF YDTTNHFLPL
DELEHSLGES AAQGAAGVVL WVSWENTRTK ESCQAIKEYM DTTLGPFILN VTSGALLCSQ
ALCSGHGRCV RRTSHPKALL LLNPASFSIQ LTPGGGPLSL RGALSLEDQA QMAVEFKCRC
YPGWQAPWCE RKSMW
