CEIP2_HUMAN
ID CEIP2_HUMAN Reviewed; 1383 AA.
AC Q9UHN6; A6H8W9; B2RTQ6; Q5T838; Q5T839; Q5T840; Q5T841; Q8NBP6; Q9P2D5;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cell surface hyaluronidase {ECO:0000303|PubMed:28246172};
DE EC=3.2.1.35 {ECO:0000305|PubMed:28246172};
DE AltName: Full=Cell migration-inducing hyaluronidase 2 {ECO:0000312|HGNC:HGNC:11869};
DE AltName: Full=Transmembrane protein 2 {ECO:0000303|PubMed:10767548};
GN Name=CEMIP2 {ECO:0000312|HGNC:HGNC:11869};
GN Synonyms=KIAA1412 {ECO:0000303|PubMed:10718198},
GN TMEM2 {ECO:0000303|PubMed:10767548};
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), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=10767548; DOI=10.1016/s0378-1119(00)00090-1;
RA Scott D.A., Drury S., Sundstrom R.A., Bishop J., Swiderski R.E., Carmi R.,
RA Ramesh A., Elbedour K., Srikumari Srisailapathy C.R., Keats B.J.,
RA Sheffield V.C., Smith R.J.H.;
RT "Refining the DFNB7-DFNB11 deafness locus using intragenic polymorphisms in
RT a novel gene, TMEM2.";
RL Gene 246:265-274(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 579-1383.
RC TISSUE=Teratocarcinoma;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 260-GLU--ASP-262; ARG-265;
RP ASP-273; ASP-275; 281-GLU--GLU-283 AND ASP-286.
RX PubMed=28246172; DOI=10.1074/jbc.m116.770149;
RA Yamamoto H., Tobisawa Y., Inubushi T., Irie F., Oyama C., Yamaguchi Y.;
RT "A Mammalian homolog of the zebrafish transmembrane protein 2 (TMEM2) is
RT the long-sought-after cell surface hyaluronidase.";
RL J. Biol. Chem. 292:7304-7313(2017).
CC -!- FUNCTION: Cell surface hyaluronidase that mediates the initial cleavage
CC of extracellular high-molecular-weight hyaluronan into intermediate-
CC size hyaluronan of approximately 5 kDa fragments (PubMed:28246172).
CC Acts as a regulator of angiogenesis and heart morphogenesis by
CC mediating degradation of extracellular hyaluronan, thereby regulating
CC VEGF signaling (By similarity). Is very specific to hyaluronan; not
CC able to cleave chondroitin sulfate or dermatan sulfate
CC (PubMed:28246172). {ECO:0000250|UniProtKB:A3KPQ7,
CC ECO:0000269|PubMed:28246172}.
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 Evidence={ECO:0000305|PubMed:28246172};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:28246172};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-7. {ECO:0000269|PubMed:28246172};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28246172};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:28246172}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHN6-2; Sequence=VSP_041401;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10767548}.
CC -!- SIMILARITY: Belongs to the CEMIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92650.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11574.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF137030; AAF21348.1; -; mRNA.
DR EMBL; AB037833; BAA92650.2; ALT_INIT; mRNA.
DR EMBL; AL161732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62518.1; -; Genomic_DNA.
DR EMBL; BC140773; AAI40774.1; -; mRNA.
DR EMBL; BC146780; AAI46781.1; -; mRNA.
DR EMBL; AK075370; BAC11574.1; ALT_INIT; mRNA.
DR CCDS; CCDS47979.1; -. [Q9UHN6-2]
DR CCDS; CCDS6638.1; -. [Q9UHN6-1]
DR RefSeq; NP_001129292.1; NM_001135820.1. [Q9UHN6-2]
DR RefSeq; NP_037522.1; NM_013390.2. [Q9UHN6-1]
DR RefSeq; XP_005251926.1; XM_005251869.4. [Q9UHN6-1]
DR AlphaFoldDB; Q9UHN6; -.
DR SMR; Q9UHN6; -.
DR BioGRID; 117188; 121.
DR IntAct; Q9UHN6; 25.
DR MINT; Q9UHN6; -.
DR STRING; 9606.ENSP00000366243; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR GlyConnect; 1851; 3 N-Linked glycans (2 sites).
DR GlyGen; Q9UHN6; 9 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q9UHN6; -.
DR PhosphoSitePlus; Q9UHN6; -.
DR SwissPalm; Q9UHN6; -.
DR BioMuta; TMEM2; -.
DR DMDM; 74753330; -.
DR EPD; Q9UHN6; -.
DR jPOST; Q9UHN6; -.
DR MassIVE; Q9UHN6; -.
DR MaxQB; Q9UHN6; -.
DR PaxDb; Q9UHN6; -.
DR PeptideAtlas; Q9UHN6; -.
DR PRIDE; Q9UHN6; -.
DR ProteomicsDB; 84383; -. [Q9UHN6-1]
DR ProteomicsDB; 84384; -. [Q9UHN6-2]
DR Antibodypedia; 43356; 72 antibodies from 19 providers.
DR DNASU; 23670; -.
DR Ensembl; ENST00000377044.9; ENSP00000366243.4; ENSG00000135048.14. [Q9UHN6-1]
DR Ensembl; ENST00000377066.9; ENSP00000366266.5; ENSG00000135048.14. [Q9UHN6-2]
DR GeneID; 23670; -.
DR KEGG; hsa:23670; -.
DR MANE-Select; ENST00000377044.9; ENSP00000366243.4; NM_013390.3; NP_037522.1.
DR UCSC; uc010mos.3; human. [Q9UHN6-1]
DR CTD; 23670; -.
DR DisGeNET; 23670; -.
DR GeneCards; CEMIP2; -.
DR HGNC; HGNC:11869; CEMIP2.
DR HPA; ENSG00000135048; Tissue enhanced (parathyroid gland, placenta).
DR MalaCards; CEMIP2; -.
DR MIM; 605835; gene.
DR neXtProt; NX_Q9UHN6; -.
DR OpenTargets; ENSG00000135048; -.
DR PharmGKB; PA36570; -.
DR VEuPathDB; HostDB:ENSG00000135048; -.
DR eggNOG; ENOG502QUM7; Eukaryota.
DR GeneTree; ENSGT00940000153636; -.
DR HOGENOM; CLU_005606_0_0_1; -.
DR InParanoid; Q9UHN6; -.
DR OMA; KDVSNCM; -.
DR PhylomeDB; Q9UHN6; -.
DR TreeFam; TF316575; -.
DR PathwayCommons; Q9UHN6; -.
DR SignaLink; Q9UHN6; -.
DR BioGRID-ORCS; 23670; 14 hits in 1082 CRISPR screens.
DR ChiTaRS; TMEM2; human.
DR GenomeRNAi; 23670; -.
DR Pharos; Q9UHN6; Tbio.
DR PRO; PR:Q9UHN6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UHN6; protein.
DR Bgee; ENSG00000135048; Expressed in upper lobe of left lung and 165 other tissues.
DR ExpressionAtlas; Q9UHN6; baseline and differential.
DR Genevisible; Q9UHN6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
DR GO; GO:1903670; P:regulation of sprouting angiogenesis; ISS:UniProtKB.
DR CDD; cd13938; PANDER_like_TMEM2; 1.
DR InterPro; IPR019316; G8_domain.
DR InterPro; IPR039477; ILEI/PANDER_dom.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039473; TMEM2_PANDER-like.
DR Pfam; PF10162; G8; 1.
DR Pfam; PF15711; ILEI; 2.
DR SMART; SM01225; G8; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS51484; G8; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Cell membrane; Developmental protein;
KW Glycoprotein; Glycosidase; Hydrolase; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1383
FT /note="Cell surface hyaluronidase"
FT /id="PRO_0000289972"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..103
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..1383
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 121..245
FT /note="G8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00817"
FT REPEAT 669..691
FT /note="PbH1 1"
FT REPEAT 711..733
FT /note="PbH1 2"
FT REPEAT 791..812
FT /note="PbH1 3"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 402..464
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041401"
FT VARIANT 245
FT /note="R -> K (in dbSNP:rs25688)"
FT /id="VAR_032669"
FT VARIANT 291
FT /note="R -> H (in dbSNP:rs25689)"
FT /id="VAR_032670"
FT VARIANT 291
FT /note="R -> L (in dbSNP:rs25689)"
FT /id="VAR_062197"
FT VARIANT 291
FT /note="R -> P (in dbSNP:rs25689)"
FT /id="VAR_062198"
FT VARIANT 423
FT /note="D -> E (in dbSNP:rs25695)"
FT /id="VAR_032671"
FT VARIANT 765
FT /note="P -> S (in dbSNP:rs25692)"
FT /id="VAR_032672"
FT VARIANT 1010
FT /note="I -> V (in dbSNP:rs17057133)"
FT /id="VAR_032673"
FT VARIANT 1254
FT /note="S -> N (in dbSNP:rs2297089)"
FT /id="VAR_032674"
FT VARIANT 1280
FT /note="G -> D (in dbSNP:rs17475375)"
FT /id="VAR_032675"
FT MUTAGEN 260..262
FT /note="EKD->NKQ: Does not affect hyaluronidase activity."
FT /evidence="ECO:0000269|PubMed:28246172"
FT MUTAGEN 265
FT /note="R->A,C: Strongly decreased hyaluronidase activity."
FT /evidence="ECO:0000269|PubMed:28246172"
FT MUTAGEN 273
FT /note="D->N: Strongly decreased hyaluronidase activity."
FT /evidence="ECO:0000269|PubMed:28246172"
FT MUTAGEN 275
FT /note="D->N: Does not affect hyaluronidase activity."
FT /evidence="ECO:0000269|PubMed:28246172"
FT MUTAGEN 281..283
FT /note="ESE->QSQ: Does not affect hyaluronidase activity."
FT /evidence="ECO:0000269|PubMed:28246172"
FT MUTAGEN 286
FT /note="D->N: Strongly decreased hyaluronidase activity."
FT /evidence="ECO:0000269|PubMed:28246172"
FT CONFLICT 1223
FT /note="T -> A (in Ref. 7; BAC11574)"
FT /evidence="ECO:0000305"
FT CONFLICT 1322
FT /note="I -> V (in Ref. 7; BAC11574)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1383 AA; 154374 MW; 18954F8ADF94C317 CRC64;
MYATDSRGHS PAFLQPQNGN SRHPSGYVPG KVVPLRPPPP PKSQASAKFT SIRREDRATF
AFSPEEQQAQ RESQKQKRHK NTFICFAITS FSFFIALAII LGISSKYAPD ENCPDQNPRL
RNWDPGQDSA KQVVIKEGDM LRLTSDATVH SIVIQDGGLL VFGDNKDGSR NITLRTHYIL
IQDGGALHIG AEKCRYKSKA TITLYGKSDE GESMPTFGKK FIGVEAGGTL ELHGARKASW
TLLARTLNSS GLPFGSYTFE KDFSRGLNVR VIDQDTAKIL ESERFDTHEY RNESRRLQEF
LRFQDPGRIV AIAVGDSAAK SLLQGTIQMI QERLGSELIQ GLGYRQAWAL VGVIDGGSTS
CNESVRNYEN HSSGGKALAQ REFYTVDGQK FSVTAYSEWI EGVSLSGFRV EVVDGVKLNL
LDDVSSWKPG DQIVVASTDY SMYQAEEFTL LPCSECSHFQ VKVKETPQFL HMGEIIDGVD
MRAEVGILTR NIVIQGEVED SCYAENQCQF FDYDTFGGHI MIMKNFTSVH LSYVELKHMG
QQQMGRYPVH FHLCGDVDYK GGYRHATFVD GLSIHHSFSR CITVHGTNGL LIKDTIGFDT
LGHCFFLEDG IEQRNTLFHN LGLLTKPGTL LPTDRNNSMC TTMRDKVFGN YIPVPATDCM
AVSTFWIAHP NNNLINNAAA GSQDAGIWYL FHKEPTGESS GLQLLAKPEL TPLGIFYNNR
VHSNFKAGLF IDKGVKTTNS SAADPREYLC LDNSARFRPH QDANPEKPRV AALIDRLIAF
KNNDNGAWVR GGDIIVQNSA FADNGIGLTF ASDGSFPSDE GSSQEVSESL FVGESRNYGF
QGGQNKYVGT GGIDQKPRTL PRNRTFPIRG FQIYDGPIHL TRSTFKKYVP TPDRYSSAIG
FLMKNSWQIT PRNNISLVKF GPHVSLNVFF GKPGPWFEDC EMDGDKNSIF HDIDGSVTGY
KDAYVGRMDN YLIRHPSCVN VSKWNAVICS GTYAQVYVQT WSTQNLSMTI TRDEYPSNPM
VLRGINQKAA FPQYQPVVML EKGYTIHWNG PAPRTTFLYL VNFNKNDWIR VGLCYPSNTS
FQVTFGYLQR QNGSLSKIEE YEPVHSLEEL QRKQSERKFY FDSSTGLLFL YLKAKSHRHG
HSYCSSQGCE RVKIQAATDS KDISNCMAKA YPQYYRKPSV VKRMPAMLTG LCQGCGTRQV
VFTSDPHKSY LPVQFQSPDK AETQRGDPSV ISVNGTDFTF RSAGVLLLVV DPCSVPFRLT
EKTVFPLADV SRIEEYLKTG IPPRSIVLLS TRGEIKQLNI SHLLVPLGLA KPAHLYDKGS
TIFLGFSGNF KPSWTKLFTS PAGQGLGVLE QFIPLQLDEY GCPRATTVRR RDLELLKQAS
KAH
