GenomeNet

Database: UniProt
Entry: Q12794
LinkDB: Q12794
Original site: Q12794 
ID   HYAL1_HUMAN             Reviewed;         435 AA.
AC   Q12794; Q6FH23; Q6PIZ6; Q7KYU2; Q7LE34; Q8NFK5; Q8NFK6; Q8NFK7;
AC   Q8NFK8; Q8NFK9; Q93013; Q9UKD5; Q9UNI8;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   10-APR-2019, entry version 162.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Sekido Y., Lee C.C., Geil L., Kuzmin I., Zabarovsky E., Klein G.,
RA   Zbar B., Minna J.D., Lerman M.I.;
RT   "Construction of a 600-kilobase cosmid clone contig and generation of
RT   a transcriptional map surrounding the lung cancer tumor suppressor
RT   gene (TSG) locus on human chromosome 3p21.3: progress toward the
RT   isolation of a lung cancer TSG.";
RL   Cancer Res. 56:1487-1492(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 22-37;
RP   72-84; 248-259 AND 261-273, SUBCELLULAR LOCATION, AND TISSUE
RP   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
RT   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
RT   3p21.3, is inactivated in head and neck squamous cell carcinomas by
RT   aberrant splicing 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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   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
RT   project: 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
RP   MASS SPECTROMETRY, GLYCOSYLATION AT ASN-99; ASN-216 AND ASN-350, AND
RP   DISULFIDE 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
RT   family encoding disparate hyaluronidase activities, cause a newly
RT   described 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
CC       block the TGFB1-enhanced cell growth.
CC       {ECO:0000269|PubMed:12084718}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-
CC         beta-D-glucosamine and D-glucuronate residues in hyaluronate.;
CC         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}.
CC       Lysosome {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         Note=Enzymatically inactive.;
CC       Name=3; Synonyms=HYAl1v2;
CC         IsoId=Q12794-3; Sequence=VSP_015917;
CC         Note=Enzymatically inactive.;
CC       Name=4; Synonyms=HYAl1v3;
CC         IsoId=Q12794-4; Sequence=VSP_015918, VSP_015919;
CC         Note=Enzymatically inactive.;
CC       Name=5; Synonyms=HYAl1v4;
CC         IsoId=Q12794-5; Sequence=VSP_015916;
CC         Note=Enzymatically inactive.;
CC       Name=6; Synonyms=HYAl1v5;
CC         IsoId=Q12794-6; Sequence=VSP_015915;
CC         Note=Enzymatically inactive.;
CC       Name=7;
CC         IsoId=Q12794-7; Sequence=VSP_015921, VSP_015922;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the liver, kidney and
CC       heart. Weakly expressed in lung, placenta and skeletal muscle. No
CC       expression detected in adult brain. Isoform 1 is expressed only in
CC       bladder and prostate cancer cells, G2/G3 bladder tumor tissues and
CC       lymph node specimens showing tumor invasive tumors cells. Isoform
CC       3, isoform 4, isoform 5 and isoform 6 are expressed in normal
CC       bladder and bladder tumor tissues. {ECO:0000269|PubMed:10339581,
CC       ECO:0000269|PubMed:12084718, ECO:0000269|PubMed:9223416}.
CC   -!- DISEASE: Mucopolysaccharidosis 9 (MPS9) [MIM:601492]: A lysosomal
CC       storage disease characterized by high hyaluronan concentration in
CC       the serum. The clinical features are periarticular soft tissue
CC       masses, mild short stature and acetabular erosions, and absence of
CC       neurological or visceral involvement.
CC       {ECO:0000269|PubMed:10339581}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {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
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/HYAL1ID40903ch3p21.html";
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   UniGene; Hs.75619; -.
DR   PDB; 2PE4; X-ray; 2.00 A; A=22-435.
DR   PDBsum; 2PE4; -.
DR   ProteinModelPortal; Q12794; -.
DR   SMR; Q12794; -.
DR   BioGrid; 109603; 8.
DR   IntAct; Q12794; 2.
DR   STRING; 9606.ENSP00000266031; -.
DR   BindingDB; Q12794; -.
DR   ChEMBL; CHEMBL4528; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   iPTMnet; Q12794; -.
DR   PhosphoSitePlus; Q12794; -.
DR   BioMuta; HYAL1; -.
DR   DMDM; 74735617; -.
DR   jPOST; Q12794; -.
DR   MaxQB; Q12794; -.
DR   PaxDb; Q12794; -.
DR   PeptideAtlas; Q12794; -.
DR   PRIDE; Q12794; -.
DR   ProteomicsDB; 58936; -.
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   DNASU; 3373; -.
DR   Ensembl; ENST00000266031; ENSP00000266031; ENSG00000114378. [Q12794-1]
DR   Ensembl; ENST00000320295; ENSP00000346068; ENSG00000114378. [Q12794-1]
DR   Ensembl; ENST00000395143; ENSP00000378575; ENSG00000114378. [Q12794-2]
DR   Ensembl; ENST00000395144; ENSP00000378576; ENSG00000114378. [Q12794-1]
DR   Ensembl; ENST00000447605; ENSP00000390149; ENSG00000114378. [Q12794-5]
DR   Ensembl; ENST00000457214; ENSP00000393358; ENSG00000114378. [Q12794-3]
DR   Ensembl; ENST00000618175; ENSP00000477903; ENSG00000114378. [Q12794-1]
DR   GeneID; 3373; -.
DR   KEGG; hsa:3373; -.
DR   UCSC; uc003czm.5; human. [Q12794-1]
DR   CTD; 3373; -.
DR   DisGeNET; 3373; -.
DR   EuPathDB; HostDB:ENSG00000114378.16; -.
DR   GeneCards; HYAL1; -.
DR   HGNC; HGNC:5320; HYAL1.
DR   HPA; HPA002112; -.
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   eggNOG; ENOG410IECJ; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   GeneTree; ENSGT00950000182708; -.
DR   HOVERGEN; HBG052053; -.
DR   InParanoid; Q12794; -.
DR   KO; K01197; -.
DR   OMA; PVLPYAQ; -.
DR   OrthoDB; 1096692at2759; -.
DR   PhylomeDB; Q12794; -.
DR   TreeFam; TF321598; -.
DR   BioCyc; MetaCyc:HS03763-MONOMER; -.
DR   BRENDA; 3.2.1.35; 2681.
DR   BRENDA; 4.2.2.1; 2681.
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   SIGNOR; Q12794; -.
DR   EvolutionaryTrace; Q12794; -.
DR   GeneWiki; HYAL1; -.
DR   GenomeRNAi; 3373; -.
DR   PRO; PR:Q12794; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000114378; Expressed in 90 organ(s), highest expression level in liver.
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:0008134; F:transcription factor binding; 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   GO; GO:0046718; P:viral entry into host cell; IEA:GOC.
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; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW   Mucopolysaccharidosis; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    435       Hyaluronidase-1.
FT                                /FTId=PRO_0000042622.
FT   DOMAIN      354    430       EGF-like.
FT   ACT_SITE    131    131       Proton donor. {ECO:0000305}.
FT   CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17503783}.
FT   CARBOHYD    216    216       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17503783}.
FT   CARBOHYD    350    350       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17503783}.
FT   DISULFID     43    333       {ECO:0000269|PubMed:17503783}.
FT   DISULFID    207    221       {ECO:0000269|PubMed:17503783}.
FT   DISULFID    358    369       {ECO:0000269|PubMed:17503783}.
FT   DISULFID    363    418       {ECO:0000269|PubMed:17503783}.
FT   DISULFID    420    429       {ECO:0000269|PubMed:17503783}.
FT   VAR_SEQ       1    339       Missing (in isoform 6).
FT                                {ECO:0000303|PubMed:12084718}.
FT                                /FTId=VSP_015915.
FT   VAR_SEQ       1    259       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:12084718}.
FT                                /FTId=VSP_015916.
FT   VAR_SEQ       1    182       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:12084718}.
FT                                /FTId=VSP_015917.
FT   VAR_SEQ     208    209       YN -> SG (in isoform 4).
FT                                {ECO:0000303|PubMed:12084718}.
FT                                /FTId=VSP_015918.
FT   VAR_SEQ     210    435       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:12084718}.
FT                                /FTId=VSP_015919.
FT   VAR_SEQ     301    330       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12084718,
FT                                ECO:0000303|Ref.6}.
FT                                /FTId=VSP_015920.
FT   VAR_SEQ     331    336       ESCQAI -> VSLGLA (in isoform 7).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_015921.
FT   VAR_SEQ     337    435       Missing (in isoform 7).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_015922.
FT   VARIANT     268    268       E -> K (in MPS9; dbSNP:rs104893743).
FT                                {ECO:0000269|PubMed:10339581}.
FT                                /FTId=VAR_023643.
FT   CONFLICT      3      3       A -> G (in Ref. 6; CAG46731).
FT                                {ECO:0000305}.
FT   CONFLICT    191    191       R -> G (in Ref. 1; AAD53277).
FT                                {ECO:0000305}.
FT   CONFLICT    300    300       L -> Q (in Ref. 3; AAD24460).
FT                                {ECO:0000305}.
FT   STRAND       24     27       {ECO:0000244|PDB:2PE4}.
FT   STRAND       30     38       {ECO:0000244|PDB:2PE4}.
FT   HELIX        40     47       {ECO:0000244|PDB:2PE4}.
FT   STRAND       56     59       {ECO:0000244|PDB:2PE4}.
FT   STRAND       69     74       {ECO:0000244|PDB:2PE4}.
FT   STRAND       78     80       {ECO:0000244|PDB:2PE4}.
FT   HELIX        97     99       {ECO:0000244|PDB:2PE4}.
FT   HELIX       102    116       {ECO:0000244|PDB:2PE4}.
FT   STRAND      124    128       {ECO:0000244|PDB:2PE4}.
FT   HELIX       137    139       {ECO:0000244|PDB:2PE4}.
FT   HELIX       142    144       {ECO:0000244|PDB:2PE4}.
FT   HELIX       145    158       {ECO:0000244|PDB:2PE4}.
FT   STRAND      159    161       {ECO:0000244|PDB:2PE4}.
FT   HELIX       164    193       {ECO:0000244|PDB:2PE4}.
FT   STRAND      197    202       {ECO:0000244|PDB:2PE4}.
FT   HELIX       223    230       {ECO:0000244|PDB:2PE4}.
FT   HELIX       233    238       {ECO:0000244|PDB:2PE4}.
FT   STRAND      240    243       {ECO:0000244|PDB:2PE4}.
FT   HELIX       250    252       {ECO:0000244|PDB:2PE4}.
FT   HELIX       258    275       {ECO:0000244|PDB:2PE4}.
FT   HELIX       300    304       {ECO:0000244|PDB:2PE4}.
FT   HELIX       307    312       {ECO:0000244|PDB:2PE4}.
FT   STRAND      316    321       {ECO:0000244|PDB:2PE4}.
FT   HELIX       324    326       {ECO:0000244|PDB:2PE4}.
FT   STRAND      327    329       {ECO:0000244|PDB:2PE4}.
FT   HELIX       330    342       {ECO:0000244|PDB:2PE4}.
FT   HELIX       344    362       {ECO:0000244|PDB:2PE4}.
FT   STRAND      366    371       {ECO:0000244|PDB:2PE4}.
FT   TURN        384    386       {ECO:0000244|PDB:2PE4}.
FT   STRAND      387    391       {ECO:0000244|PDB:2PE4}.
FT   HELIX       393    395       {ECO:0000244|PDB:2PE4}.
FT   STRAND      398    402       {ECO:0000244|PDB:2PE4}.
FT   HELIX       406    415       {ECO:0000244|PDB:2PE4}.
FT   STRAND      416    420       {ECO:0000244|PDB:2PE4}.
FT   TURN        426    429       {ECO:0000244|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
//
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