OFUT2_HUMAN
ID OFUT2_HUMAN Reviewed; 429 AA.
AC Q9Y2G5; Q6PJV1; Q7Z4N0; Q8WWU6; Q9BQS4; Q9BQS5; Q9UFY3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=GDP-fucose protein O-fucosyltransferase 2;
DE EC=2.4.1.221 {ECO:0000269|PubMed:16464858, ECO:0000269|PubMed:22588082};
DE AltName: Full=Peptide-O-fucosyltransferase 2;
DE Short=O-FucT-2;
DE Flags: Precursor;
GN Name=POFUT2; Synonyms=C21orf80, FUT13, KIAA0958;
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] (ISOFORMS A; B AND C), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=15233996; DOI=10.1016/j.ygeno.2004.04.002;
RA Menzel O., Vellai T., Takacs-Vellai K., Reymond A., Mueller F.,
RA Antonarakis S.E., Guipponi M.;
RT "The Caenorhabditis elegans ortholog of C21orf80, a potential new protein
RT O-fucosyltransferase, is required for normal development.";
RL Genomics 84:320-330(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RX PubMed=12966037; DOI=10.1093/glycob/cwg113;
RA Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C., Oriol R.;
RT "A new superfamily of protein-O-fucosyltransferases, alpha2-
RT fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and
RT identification of conserved peptide motifs.";
RL Glycobiology 13:1C-5C(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C).
RC TISSUE=Brain;
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 FUNCTION.
RX PubMed=11067851; DOI=10.1074/jbc.m008073200;
RA Hofsteenge J., Huwiler K.G., Macek B., Hess D., Lawler J., Mosher D.F.,
RA Peter-Katalinic J.;
RT "C-mannosylation and O-fucosylation of the thrombospondin type 1 module.";
RL J. Biol. Chem. 276:6485-6498(2001).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=16464858; DOI=10.1074/jbc.m511974200;
RA Luo Y., Nita-Lazar A., Haltiwanger R.S.;
RT "Two distinct pathways for O-fucosylation of epidermal growth factor-like
RT or thrombospondin type 1 repeats.";
RL J. Biol. Chem. 281:9385-9392(2006).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLU-395 AND GLU-396.
RX PubMed=17395589; DOI=10.1074/jbc.m700317200;
RA Ricketts L.M., Dlugosz M., Luther K.B., Haltiwanger R.S., Majerus E.M.;
RT "O-fucosylation is required for ADAMTS13 secretion.";
RL J. Biol. Chem. 282:17014-17023(2007).
RN [10]
RP FUNCTION.
RX PubMed=17395588; DOI=10.1074/jbc.m701065200;
RA Wang L.W., Dlugosz M., Somerville R.P., Raed M., Haltiwanger R.S.,
RA Apte S.S.;
RT "O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1
RT regulates secretion: implications for the ADAMTS superfamily.";
RL J. Biol. Chem. 282:17024-17031(2007).
RN [11]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-21, AND
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 [12]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-429 IN COMPLEX WITH GDP-FUCOSE,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, MUTAGENESIS OF GLU-54; TRP-92; TRP-152; TRP-273;
RP ARG-294; ASP-297 AND GLU-396, GLYCOSYLATION AT ASN-189 AND ASN-259, AND
RP DISULFIDE BONDS.
RX PubMed=22588082; DOI=10.1038/emboj.2012.143;
RA Chen C.I., Keusch J.J., Klein D., Hess D., Hofsteenge J., Gut H.;
RT "Structure of human POFUT2: insights into thrombospondin type 1 repeat fold
RT and O-fucosylation.";
RL EMBO J. 31:3183-3197(2012).
CC -!- FUNCTION: Catalyzes the reaction that attaches fucose through an O-
CC glycosidic linkage to a conserved serine or threonine residue in the
CC consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats
CC (TSRs) where C1 and C2 are the first and second cysteines of the
CC repeat, respectively (PubMed:22588082). O-fucosylates members of
CC several protein families including the ADAMTS, the thrombospondin (TSP)
CC and spondin families (Probable) (PubMed:17395588). Required for the
CC proper secretion of ADAMTS family members such as ADAMTSL1 and ADAMTS13
CC (PubMed:17395589, PubMed:17395588). The O-fucosylation of TSRs is also
CC required for restricting epithelial to mesenchymal transition (EMT),
CC maintaining the correct patterning of mesoderm and localization of the
CC definite endoderm (By similarity). {ECO:0000250|UniProtKB:Q8VHI3,
CC ECO:0000269|PubMed:17395588, ECO:0000269|PubMed:17395589,
CC ECO:0000269|PubMed:22588082, ECO:0000305|PubMed:11067851,
CC ECO:0000305|PubMed:16464858}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-seryl-[protein] = 3-O-(alpha-L-fucosyl)-
CC L-seryl-[protein] + GDP + H(+); Xref=Rhea:RHEA:63644, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:17914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189632; EC=2.4.1.221;
CC Evidence={ECO:0000269|PubMed:16464858, ECO:0000269|PubMed:22588082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63645;
CC Evidence={ECO:0000269|PubMed:16464858, ECO:0000269|PubMed:22588082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + L-threonyl-[protein] = 3-O-(alpha-L-
CC fucosyl)-L-threonyl-[protein] + GDP + H(+); Xref=Rhea:RHEA:70491,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:17915, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:189631; EC=2.4.1.221;
CC Evidence={ECO:0000269|PubMed:16464858, ECO:0000269|PubMed:22588082};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70492;
CC Evidence={ECO:0000269|PubMed:16464858, ECO:0000269|PubMed:22588082};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA and by Zn(2+).
CC {ECO:0000269|PubMed:22588082}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.8 uM for GDP-fucose {ECO:0000269|PubMed:22588082};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:16464858, ECO:0000269|PubMed:22588082}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:15233996}. Golgi apparatus
CC {ECO:0000269|PubMed:15233996}. Note=Mainly located in the endoplasmic
CC reticulum. {ECO:0000269|PubMed:15233996}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C;
CC IsoId=Q9Y2G5-3; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9Y2G5-1; Sequence=VSP_003832;
CC Name=B;
CC IsoId=Q9Y2G5-2; Sequence=VSP_003833, VSP_003834;
CC -!- TISSUE SPECIFICITY: Isoform A is expressed in fetal liver and
CC peripheral blood lymphocytes. Isoform B is expressed in spleen, lung,
CC testis, bone marrow, thymus, pancreas, prostate, fetal brain, fetal
CC liver and fetal kidney. Isoform C is expressed in brain, heart, spleen,
CC liver, lung, stomach, testis, placenta, skin, thymus, pancreas, mammary
CC gland, prostate, fetal brain, fetal liver and fetal heart.
CC {ECO:0000269|PubMed:15233996}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 68 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76802.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB90496.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Peptide-
CC O-fucosyltransferase 2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_610";
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DR EMBL; AJ302080; CAC24557.1; -; mRNA.
DR EMBL; AJ302079; CAC24556.1; -; mRNA.
DR EMBL; AY066015; AAL47681.2; -; mRNA.
DR EMBL; AJ575591; CAE01472.1; -; mRNA.
DR EMBL; AB023175; BAA76802.1; ALT_INIT; mRNA.
DR EMBL; AL110285; CAB53715.2; -; mRNA.
DR EMBL; AL163301; CAB90496.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC011044; AAH11044.1; -; mRNA.
DR EMBL; BC064623; AAH64623.1; -; mRNA.
DR CCDS; CCDS13719.1; -. [Q9Y2G5-3]
DR CCDS; CCDS13721.1; -. [Q9Y2G5-1]
DR RefSeq; NP_056042.1; NM_015227.4. [Q9Y2G5-1]
DR RefSeq; NP_598368.2; NM_133635.4. [Q9Y2G5-3]
DR PDB; 4AP5; X-ray; 3.00 A; A/B=22-429.
DR PDB; 4AP6; X-ray; 3.40 A; A/B/C/D=37-429.
DR PDBsum; 4AP5; -.
DR PDBsum; 4AP6; -.
DR AlphaFoldDB; Q9Y2G5; -.
DR SMR; Q9Y2G5; -.
DR BioGRID; 116876; 7.
DR IntAct; Q9Y2G5; 4.
DR STRING; 9606.ENSP00000339613; -.
DR CAZy; GT68; Glycosyltransferase Family 68.
DR GlyGen; Q9Y2G5; 3 sites.
DR iPTMnet; Q9Y2G5; -.
DR PhosphoSitePlus; Q9Y2G5; -.
DR BioMuta; POFUT2; -.
DR DMDM; 59803123; -.
DR EPD; Q9Y2G5; -.
DR jPOST; Q9Y2G5; -.
DR MassIVE; Q9Y2G5; -.
DR MaxQB; Q9Y2G5; -.
DR PaxDb; Q9Y2G5; -.
DR PeptideAtlas; Q9Y2G5; -.
DR PRIDE; Q9Y2G5; -.
DR ProteomicsDB; 85769; -. [Q9Y2G5-3]
DR ProteomicsDB; 85770; -. [Q9Y2G5-1]
DR ProteomicsDB; 85771; -. [Q9Y2G5-2]
DR Antibodypedia; 10462; 302 antibodies from 29 providers.
DR DNASU; 23275; -.
DR Ensembl; ENST00000331343.11; ENSP00000329682.7; ENSG00000186866.17. [Q9Y2G5-1]
DR Ensembl; ENST00000334538.13; ENSP00000335427.9; ENSG00000186866.17. [Q9Y2G5-2]
DR Ensembl; ENST00000349485.10; ENSP00000339613.5; ENSG00000186866.17. [Q9Y2G5-3]
DR GeneID; 23275; -.
DR KEGG; hsa:23275; -.
DR MANE-Select; ENST00000349485.10; ENSP00000339613.5; NM_133635.6; NP_598368.2.
DR UCSC; uc002zhb.4; human. [Q9Y2G5-3]
DR CTD; 23275; -.
DR DisGeNET; 23275; -.
DR GeneCards; POFUT2; -.
DR HGNC; HGNC:14683; POFUT2.
DR HPA; ENSG00000186866; Low tissue specificity.
DR MIM; 610249; gene.
DR neXtProt; NX_Q9Y2G5; -.
DR OpenTargets; ENSG00000186866; -.
DR PharmGKB; PA25867; -.
DR VEuPathDB; HostDB:ENSG00000186866; -.
DR eggNOG; ENOG502QPS6; Eukaryota.
DR GeneTree; ENSGT00390000007989; -.
DR HOGENOM; CLU_033856_0_0_1; -.
DR InParanoid; Q9Y2G5; -.
DR OMA; YILYDVN; -.
DR OrthoDB; 654070at2759; -.
DR PhylomeDB; Q9Y2G5; -.
DR TreeFam; TF314337; -.
DR BRENDA; 2.4.1.221; 2681.
DR PathwayCommons; Q9Y2G5; -.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q9Y2G5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 23275; 15 hits in 1075 CRISPR screens.
DR GenomeRNAi; 23275; -.
DR Pharos; Q9Y2G5; Tbio.
DR PRO; PR:Q9Y2G5; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9Y2G5; protein.
DR Bgee; ENSG00000186866; Expressed in right uterine tube and 183 other tissues.
DR ExpressionAtlas; Q9Y2G5; baseline and differential.
DR Genevisible; Q9Y2G5; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0046922; F:peptide-O-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006004; P:fucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:1903334; P:positive regulation of protein folding; IMP:CACAO.
DR GO; GO:0036066; P:protein O-linked fucosylation; IDA:UniProtKB.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0051046; P:regulation of secretion; IDA:UniProtKB.
DR InterPro; IPR019378; GDP-Fuc_O-FucTrfase.
DR InterPro; IPR045130; OFUT2-like.
DR PANTHER; PTHR13398; PTHR13398; 1.
DR Pfam; PF10250; O-FucT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carbohydrate metabolism;
KW Disulfide bond; Endoplasmic reticulum; Fucose metabolism; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Reference proteome; Signal;
KW Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT CHAIN 22..429
FT /note="GDP-fucose protein O-fucosyltransferase 2"
FT /id="PRO_0000012154"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:22588082"
FT BINDING 53..57
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000269|PubMed:22588082,
FT ECO:0007744|PDB:4AP6"
FT BINDING 292..294
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000269|PubMed:22588082,
FT ECO:0007744|PDB:4AP6"
FT BINDING 371
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000269|PubMed:22588082,
FT ECO:0007744|PDB:4AP6"
FT BINDING 388..389
FT /ligand="GDP-beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:57273"
FT /evidence="ECO:0000269|PubMed:22588082,
FT ECO:0007744|PDB:4AP6"
FT SITE 396
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000269|PubMed:17395589,
FT ECO:0000269|PubMed:22588082"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22588082"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22588082"
FT DISULFID 161..192
FT /evidence="ECO:0000269|PubMed:22588082,
FT ECO:0007744|PDB:4AP5, ECO:0007744|PDB:4AP6"
FT DISULFID 412..419
FT /evidence="ECO:0000269|PubMed:22588082,
FT ECO:0007744|PDB:4AP5, ECO:0007744|PDB:4AP6"
FT VAR_SEQ 379..380
FT /note="RF -> SS (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15233996,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_003833"
FT VAR_SEQ 380..429
FT /note="FFIGTSVSTFSFRIHEEREILGLDPKTTYNRFCGDQEKACEQPTHWKITY
FT -> CLPTSLSAESGSGGFQRFFCPKYSVSEQMVACVHSGHFHTVCLLV (in
FT isoform A)"
FT /evidence="ECO:0000303|PubMed:10231032,
FT ECO:0000303|PubMed:15233996"
FT /id="VSP_003832"
FT VAR_SEQ 381..429
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15233996,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_003834"
FT MUTAGEN 54
FT /note="E->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22588082"
FT MUTAGEN 92
FT /note="W->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22588082"
FT MUTAGEN 152
FT /note="W->A: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:22588082"
FT MUTAGEN 273
FT /note="W->A: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:22588082"
FT MUTAGEN 294
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22588082"
FT MUTAGEN 297
FT /note="D->A: Reduces enzyme activity."
FT /evidence="ECO:0000269|PubMed:22588082"
FT MUTAGEN 395
FT /note="E->A: No enhanced secretion of ADASMTS13; when
FT associated with A-396."
FT /evidence="ECO:0000269|PubMed:17395589"
FT MUTAGEN 396
FT /note="E->A: Reduces enzyme activity. No enhanced secretion
FT of ADASMTS13; when associated with A-396."
FT /evidence="ECO:0000269|PubMed:17395589,
FT ECO:0000269|PubMed:22588082"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 56..74
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 129..141
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 199..202
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 244..258
FT /evidence="ECO:0007829|PDB:4AP5"
FT TURN 262..266
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:4AP5"
FT TURN 296..302
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 309..323
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:4AP6"
FT HELIX 356..376
FT /evidence="ECO:0007829|PDB:4AP5"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:4AP5"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:4AP5"
SQ SEQUENCE 429 AA; 49976 MW; 36A4213D905AFFD1 CRC64;
MATLSFVFLL LGAVSWPPAS ASGQEFWPGQ SAADILSGAA SRRRYLLYDV NPPEGFNLRR
DVYIRIASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV RIPWSEFFDL PSLNKNIPVI
EYEQFIAESG GPFIDQVYVL QSYAEGWKEG TWEEKVDERP CIDQLLYSQD KHEYYRGWFW
GYEETRGLNV SCLSVQGSAS IVAPLLLRNT SARSVMLDRA ENLLHDHYGG KEYWDTRRSM
VFARHLREVG DEFRSRHLNS TDDADRIPFQ EDWMKMKVKL GSALGGPYLG VHLRRKDFIW
GHRQDVPSLE GAVRKIRSLM KTHRLDKVFV ATDAVRKEYE ELKKLLPEMV RFEPTWEELE
LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL GLDPKTTYNR FCGDQEKACE
QPTHWKITY
