GenomeNet

Database: UniProt
Entry: Q12891
LinkDB: Q12891
Original site: Q12891 
ID   HYAL2_HUMAN             Reviewed;         473 AA.
AC   Q12891; B3KRZ2; O15177; Q9BW29;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 4.
DT   10-APR-2019, entry version 174.
DE   RecName: Full=Hyaluronidase-2;
DE            Short=Hyal-2;
DE            EC=3.2.1.35;
DE   AltName: Full=Hyaluronoglucosaminidase-2;
DE   AltName: Full=Lung carcinoma protein 2;
DE            Short=LuCa-2;
DE   Flags: Precursor;
GN   Name=HYAL2; Synonyms=LUCA2;
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], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
RP   ALA-18.
RX   PubMed=9712871; DOI=10.1074/jbc.273.35.22466;
RA   Lepperdinger G., Strobl B., Kreil G.;
RT   "HYAL2, a human gene expressed in many cells, encodes a lysosomal
RT   hyaluronidase with a novel type of specificity.";
RL   J. Biol. Chem. 273:22466-22470(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RA   Chen J., Bader S., Latif F., Duh F.-M., Lerman M.I., Minna J.D.;
RT   "LUCA2 (HYAL2, lysosomal hyaluronidase) a novel human cDNA with
RT   homology to human PH-20 gene is homozygously deleted in small cell
RT   lung cancer and located in 3p21.3.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-18.
RC   TISSUE=Placenta, and Synovium;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-18.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-18.
RC   TISSUE=Kidney;
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-473, AND VARIANT ALA-18.
RC   TISSUE=Brain;
RA   Yu W., Gibbs R.A.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   REVIEW.
RX   PubMed=11731268; DOI=10.1016/S0945-053X(01)00170-6;
RA   Lepperdinger G., Mullegger J., Kreil G.;
RT   "Hyal2 -- less active, but more versatile?";
RL   Matrix Biol. 20:509-514(2001).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11296287; DOI=10.1073/pnas.071572898;
RA   Rai S.K., Duh F.-M., Vigdorovich V., Danilkovitch-Miagkova A.,
RA   Lerman M.I., Miller A.D.;
RT   "Candidate tumor suppressor HYAL2 is a glycosylphosphatidylinositol
RT   (GPI)-anchored cell-surface receptor for jaagsiekte sheep retrovirus,
RT   the envelope protein of which mediates oncogenic transformation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4443-4448(2001).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH MST1R.
RX   PubMed=12676986; DOI=10.1073/pnas.0837136100;
RA   Danilkovitch-Miagkova A., Duh F.-M., Kuzmin I., Angeloni D.,
RA   Liu S.-L., Miller A.D., Lerman M.I.;
RT   "Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and
RT   mediates transformation of epithelial cells by jaagsiekte sheep
RT   retrovirus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4580-4585(2003).
CC   -!- FUNCTION: Hydrolyzes high molecular weight hyaluronic acid to
CC       produce an intermediate-sized product which is further hydrolyzed
CC       by sperm hyaluronidase to give small oligosaccharides. Displays
CC       very low levels of activity. Associates with and negatively
CC       regulates MST1R. {ECO:0000269|PubMed:11296287,
CC       ECO:0000269|PubMed:12676986, ECO:0000269|PubMed:9712871}.
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   -!- SUBUNIT: Interacts with MST1R. {ECO:0000269|PubMed:12676986}.
CC   -!- INTERACTION:
CC       Q13643:FHL3; NbExp=3; IntAct=EBI-2806068, EBI-741101;
CC       Q9BYR7:KRTAP3-2; NbExp=3; IntAct=EBI-2806068, EBI-751260;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11296287};
CC       Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:11296287}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. No expression detected in
CC       adult brain. {ECO:0000269|PubMed:9712871}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be lysosomal. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC28656.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/HYAL2ID40904ch3p21.html";
DR   EMBL; AJ000099; CAA03924.1; -; mRNA.
DR   EMBL; U09577; AAC62823.1; -; mRNA.
DR   EMBL; AK092449; BAG52554.1; -; mRNA.
DR   EMBL; AK127945; BAG54602.1; -; mRNA.
DR   EMBL; AC002455; AAB67045.1; -; Genomic_DNA.
DR   EMBL; CH471055; EAW65092.1; -; Genomic_DNA.
DR   EMBL; BC000692; AAH00692.1; -; mRNA.
DR   EMBL; AF070608; AAC28656.1; ALT_INIT; mRNA.
DR   CCDS; CCDS2818.1; -.
DR   RefSeq; NP_003764.3; NM_003773.4.
DR   RefSeq; NP_149348.2; NM_033158.4.
DR   RefSeq; XP_005265581.1; XM_005265524.2.
DR   RefSeq; XP_005265582.1; XM_005265525.2.
DR   UniGene; Hs.76873; -.
DR   ProteinModelPortal; Q12891; -.
DR   SMR; Q12891; -.
DR   BioGrid; 114239; 15.
DR   IntAct; Q12891; 13.
DR   STRING; 9606.ENSP00000401853; -.
DR   CAZy; GH56; Glycoside Hydrolase Family 56.
DR   iPTMnet; Q12891; -.
DR   PhosphoSitePlus; Q12891; -.
DR   BioMuta; HYAL2; -.
DR   DMDM; 311033483; -.
DR   EPD; Q12891; -.
DR   jPOST; Q12891; -.
DR   MaxQB; Q12891; -.
DR   PaxDb; Q12891; -.
DR   PeptideAtlas; Q12891; -.
DR   PRIDE; Q12891; -.
DR   ProteomicsDB; 59006; -.
DR   DNASU; 8692; -.
DR   Ensembl; ENST00000357750; ENSP00000350387; ENSG00000068001.
DR   Ensembl; ENST00000395139; ENSP00000378571; ENSG00000068001.
DR   Ensembl; ENST00000442581; ENSP00000406657; ENSG00000068001.
DR   Ensembl; ENST00000447092; ENSP00000401853; ENSG00000068001.
DR   GeneID; 8692; -.
DR   KEGG; hsa:8692; -.
DR   UCSC; uc003czv.4; human.
DR   CTD; 8692; -.
DR   DisGeNET; 8692; -.
DR   EuPathDB; HostDB:ENSG00000068001.13; -.
DR   GeneCards; HYAL2; -.
DR   H-InvDB; HIX0003314; -.
DR   HGNC; HGNC:5321; HYAL2.
DR   HPA; HPA036436; -.
DR   MIM; 603551; gene.
DR   neXtProt; NX_Q12891; -.
DR   OpenTargets; ENSG00000068001; -.
DR   Orphanet; 508476; Cleft lip and palate-craniofacial dysmorphism-congenital heart defect-hearing loss syndrome.
DR   PharmGKB; PA29572; -.
DR   eggNOG; ENOG410IECJ; Eukaryota.
DR   eggNOG; ENOG410XPZT; LUCA.
DR   GeneTree; ENSGT00950000182708; -.
DR   HOGENOM; HOG000015133; -.
DR   HOVERGEN; HBG052053; -.
DR   InParanoid; Q12891; -.
DR   KO; K01197; -.
DR   OMA; WGGEQCQ; -.
DR   OrthoDB; 1096692at2759; -.
DR   PhylomeDB; Q12891; -.
DR   TreeFam; TF321598; -.
DR   BioCyc; MetaCyc:HS00926-MONOMER; -.
DR   BRENDA; 3.2.1.35; 2681.
DR   BRENDA; 4.2.2.1; 2681.
DR   Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
DR   SignaLink; Q12891; -.
DR   ChiTaRS; HYAL2; human.
DR   GeneWiki; HYAL2; -.
DR   GenomeRNAi; 8692; -.
DR   PRO; PR:Q12891; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000068001; Expressed in 208 organ(s), highest expression level in right lung.
DR   ExpressionAtlas; Q12891; baseline and differential.
DR   Genevisible; Q12891; HS.
DR   GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:BHF-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; NAS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR   GO; GO:0005902; C:microvillus; IDA:BHF-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISS:BHF-UCL.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
DR   GO; GO:0033906; F:hyaluronoglucuronidase activity; IDA:UniProtKB.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:UniProtKB.
DR   GO; GO:0030294; F:receptor signaling protein tyrosine kinase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0050431; F:transforming growth factor beta binding; ISS:BHF-UCL.
DR   GO; GO:0001618; F:virus receptor 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:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
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:0051607; P:defense response to virus; IEA:Ensembl.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IDA:UniProtKB.
DR   GO; GO:0006027; P:glycosaminoglycan catabolic process; IDA:UniProtKB.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
DR   GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR   GO; GO:0042117; P:monocyte activation; IDA:UniProtKB.
DR   GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR   GO; GO:0060586; P:multicellular organismal iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR   GO; GO:0010764; P:negative regulation of fibroblast migration; IDA:UniProtKB.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
DR   GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:UniProtKB.
DR   GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR   GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IDA:UniProtKB.
DR   GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IDA:UniProtKB.
DR   GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IDA:UniProtKB.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR   GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR   GO; GO:0070295; P:renal water absorption; ISS:UniProtKB.
DR   GO; GO:0046677; P:response to antibiotic; IEP: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:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR   GO; GO:0019087; P:transformation of host cell by virus; IDA:UniProtKB.
DR   GO; GO:0046718; P:viral entry into host cell; ISS: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; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein;
KW   Membrane; Polymorphism; Receptor; Reference proteome; Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    448       Hyaluronidase-2.
FT                                /FTId=PRO_0000012099.
FT   PROPEP      449    473       Removed in mature form. {ECO:0000255}.
FT                                /FTId=PRO_0000012100.
FT   DOMAIN      361    439       EGF-like.
FT   ACT_SITE    135    135       Proton donor. {ECO:0000250}.
FT   LIPID       448    448       GPI-anchor amidated glycine.
FT                                {ECO:0000255}.
FT   CARBOHYD     74     74       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    357    357       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     47    340       {ECO:0000250}.
FT   DISULFID    211    227       {ECO:0000250}.
FT   DISULFID    365    376       {ECO:0000250}.
FT   DISULFID    370    427       {ECO:0000250}.
FT   DISULFID    429    438       {ECO:0000250}.
FT   VARIANT      18     18       S -> A (in dbSNP:rs709210).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:9712871,
FT                                ECO:0000269|Ref.5, ECO:0000269|Ref.7}.
FT                                /FTId=VAR_028170.
FT   VARIANT     418    418       I -> L (in dbSNP:rs35455589).
FT                                /FTId=VAR_061193.
FT   CONFLICT    261    262       SR -> AL (in Ref. 1; CAA03924).
FT                                {ECO:0000305}.
FT   CONFLICT    301    302       RL -> C (in Ref. 1; CAA03924).
FT                                {ECO:0000305}.
FT   CONFLICT    375    375       Missing (in Ref. 1; CAA03924).
FT                                {ECO:0000305}.
FT   CONFLICT    378    379       RR -> PG (in Ref. 1; CAA03924).
FT                                {ECO:0000305}.
FT   CONFLICT    450    450       S -> N (in Ref. 1; CAA03924).
FT                                {ECO:0000305}.
SQ   SEQUENCE   473 AA;  53860 MW;  A8302738478BFE61 CRC64;
     MRAGPGPTVT LALVLAVSWA MELKPTAPPI FTGRPFVVAW DVPTQDCGPR LKVPLDLNAF
     DVQASPNEGF VNQNITIFYR DRLGLYPRFD SAGRSVHGGV PQNVSLWAHR KMLQKRVEHY
     IRTQESAGLA VIDWEDWRPV WVRNWQDKDV YRRLSRQLVA SRHPDWPPDR IVKQAQYEFE
     FAAQQFMLET LRYVKAVRPR HLWGFYLFPD CYNHDYVQNW ESYTGRCPDV EVARNDQLAW
     LWAESTALFP SVYLDETLAS SRHGRNFVSF RVQEALRVAR THHANHALPV YVFTRPTYSR
     RLTGLSEMDL ISTIGESAAL GAAGVILWGD AGYTTSTETC QYLKDYLTRL LVPYVVNVSW
     ATQYCSRAQC HGHGRCVRRN PSASTFLHLS TNSFRLVPGH APGEPQLRPV GELSWADIDH
     LQTHFRCQCY LGWSGEQCQW DHRQAAGGAS EAWAGSHLTS LLALAALAFT WTL
//
DBGET integrated database retrieval system