ACE2_RAT
ID ACE2_RAT Reviewed; 805 AA.
AC Q5EGZ1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Angiotensin-converting enzyme 2;
DE EC=3.4.17.23 {ECO:0000250|UniProtKB:Q9BYF1};
DE AltName: Full=ACE-related carboxypeptidase;
DE EC=3.4.17.- {ECO:0000250|UniProtKB:Q9BYF1};
DE Contains:
DE RecName: Full=Processed angiotensin-converting enzyme 2;
DE Flags: Precursor;
GN Name=Ace2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND LACK OF INTERACTION WITH SARS-COV SPIKE
RP GLYCOPROTEIN.
RC STRAIN=Sprague-Dawley;
RX PubMed=15452268; DOI=10.1128/jvi.78.20.11429-11433.2004;
RA Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M.,
RA Sullivan J.L., Farzan M., Choe H.;
RT "Efficient replication of severe acute respiratory syndrome coronavirus in
RT mouse cells is limited by murine angiotensin-converting enzyme 2.";
RL J. Virol. 78:11429-11433(2004).
RN [2]
RP FUNCTION, AND INDUCTION.
RX PubMed=12075344; DOI=10.1038/nature00786;
RA Crackower M.A., Sarao R., Oudit G.Y., Yagil C., Kozieradzki I.,
RA Scanga S.E., Oliveira-dos-Santos A.J., da Costa J., Zhang L., Pei Y.,
RA Scholey J., Ferrario C.M., Manoukian A.S., Chappell M.C., Backx P.H.,
RA Yagil Y., Penninger J.M.;
RT "Angiotensin-converting enzyme 2 is an essential regulator of heart
RT function.";
RL Nature 417:822-828(2002).
RN [3]
RP ACTIVITY REGULATION, GLYCOSYLATION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15231706; DOI=10.1210/en.2004-0443;
RA Douglas G.C., O'Bryan M.K., Hedger M.P., Lee D.K.L., Yarski M.A.,
RA Smith A.I., Lew R.A.;
RT "The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is
RT selectively expressed by adult Leydig cells of the testis.";
RL Endocrinology 145:4703-4711(2004).
RN [4]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15671045; DOI=10.1093/eurheartj/ehi114;
RA Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S., Lu S.,
RA Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E., Johnston C.I.;
RT "Myocardial infarction increases ACE2 expression in rat and humans.";
RL Eur. Heart J. 26:369-375(2005).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15949646; DOI=10.1016/j.peptides.2005.01.009;
RA Gembardt F., Sterner-Kock A., Imboden H., Spalteholz M., Reibitz F.,
RA Schultheiss H.-P., Siems W.-E., Walther T.;
RT "Organ-specific distribution of ACE2 mRNA and correlating peptidase
RT activity in rodents.";
RL Peptides 26:1270-1277(2005).
CC -!- FUNCTION: Essential counter-regulatory carboxypeptidase of the renin-
CC angiotensin hormone system that is a critical regulator of blood
CC volume, systemic vascular resistance, and thus cardiovascular
CC homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino
CC acid peptide with anti-hypertrophic effects in cardiomyocytes, and
CC angiotensin II to angiotensin 1-7, which then acts as a beneficial
CC vasodilator and anti-proliferation agent, counterbalancing the actions
CC of the vasoconstrictor angiotensin II. Also removes the C-terminal
CC residue from three other vasoactive peptides, neurotensin, kinetensin,
CC and des-Arg bradykinin, but is not active on bradykinin. Also cleaves
CC other biological peptides, such as apelins, casomorphins and dynorphin
CC A. Plays an important role in amino acid transport by acting as binding
CC partner of amino acid transporter SLC6A19 in intestine, regulating
CC trafficking, expression on the cell surface, and its catalytic
CC activity. {ECO:0000250|UniProtKB:Q9BYF1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=angiotensin II + H2O = angiotensin-(1-7) + L-phenylalanine;
CC Xref=Rhea:RHEA:26554, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:58506, ChEBI:CHEBI:58922; EC=3.4.17.23;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26555;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=angiotensin I + H2O = angiotensin-(1-9) + L-leucine;
CC Xref=Rhea:RHEA:63532, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:147350, ChEBI:CHEBI:147351;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63533;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bradykinin(1-8) + H2O = bradykinin(1-7) + L-phenylalanine;
CC Xref=Rhea:RHEA:63536, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:133069, ChEBI:CHEBI:147352;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63537;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + neurotensin = L-leucine + neurotensin-(1-12);
CC Xref=Rhea:RHEA:63540, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:147362, ChEBI:CHEBI:147363;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63541;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + kinetensin = kinetensin-(1-8) + L-leucine;
CC Xref=Rhea:RHEA:63544, ChEBI:CHEBI:15377, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:147364, ChEBI:CHEBI:147365;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63545;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dynorphin A-(1-13) + H2O = dynorphin A-(1-12) + L-lysine;
CC Xref=Rhea:RHEA:63556, ChEBI:CHEBI:15377, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:147381, ChEBI:CHEBI:147383;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63557;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apelin-13 + H2O = apelin-12 + L-phenylalanine;
CC Xref=Rhea:RHEA:63564, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:147395, ChEBI:CHEBI:147396;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63565;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[Pyr1]apelin-13 + H2O = [Pyr1]apelin-12 + L-phenylalanine;
CC Xref=Rhea:RHEA:63604, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:147415, ChEBI:CHEBI:147416;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63605;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apelin-17 + H2O = apelin-16 + L-phenylalanine;
CC Xref=Rhea:RHEA:63608, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095,
CC ChEBI:CHEBI:147421, ChEBI:CHEBI:147422;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63609;
CC Evidence={ECO:0000250|UniProtKB:Q9BYF1};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by chloride and fluoride, but not
CC bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the ACE
CC inhibitors linosipril, captopril, enalaprilat.
CC {ECO:0000269|PubMed:15231706}.
CC -!- SUBUNIT: Homodimer. Interacts with the catalytically active form of
CC TMPRSS2 (By similarity). Interacts with SLC6A19; this interaction is
CC essential for expression and function of SLC6A19 in intestine (By
CC similarity). Interacts with ITGA5:ITGB1 (By similarity). Probably
CC interacts (via endocytic sorting signal motif) with AP2M1; the
CC interaction is inhibited by phosphorylation of Tyr-781 (By similarity).
CC Interacts (via PDZ-binding motif) with SLC9A3R1 (via PDZ domains); the
CC interaction may enhance ACE2 membrane residence (By similarity).
CC {ECO:0000250|UniProtKB:Q8R0I0, ECO:0000250|UniProtKB:Q9BYF1}.
CC -!- INTERACTION:
CC Q5EGZ1; A0A6G6A1M4: S; Xeno; NbExp=2; IntAct=EBI-25503774, EBI-26997256;
CC Q5EGZ1; A0A6M3G9R1: S; Xeno; NbExp=2; IntAct=EBI-25503774, EBI-26997195;
CC Q5EGZ1; P0DTC2: S; Xeno; NbExp=2; IntAct=EBI-25503774, EBI-25474821;
CC Q5EGZ1; P59594: S; Xeno; NbExp=2; IntAct=EBI-25503774, EBI-15582614;
CC -!- SUBCELLULAR LOCATION: [Processed angiotensin-converting enzyme 2]:
CC Secreted {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BYF1};
CC Single-pass type I membrane protein {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8R0I0}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9BYF1}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9BYF1}. Note=Detected in both cell membrane and
CC cytoplasm in neurons. {ECO:0000250|UniProtKB:Q8R0I0}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, kidney and forebrain. In
CC testis, expression is restricted to Leydig cells. In heart, expressed
CC in endothelial cells from small and large arteries, arterial smooth
CC muscle cells, and myocytes (at protein level). Ubiquitously expressed,
CC with highest levels in ileum, bladder and lung.
CC {ECO:0000269|PubMed:15231706, ECO:0000269|PubMed:15671045,
CC ECO:0000269|PubMed:15949646}.
CC -!- INDUCTION: Down-regulated in hypertensive animals. Up-regulated after
CC myocardial infarction. {ECO:0000269|PubMed:12075344,
CC ECO:0000269|PubMed:15671045}.
CC -!- DOMAIN: The cytoplasmic tail contains several linear motifs such as
CC LIR, PDZ-binding, PTB and endocytic sorting signal motifs that would
CC allow interaction with proteins that mediate endocytic trafficking and
CC autophagy. {ECO:0000250|UniProtKB:Q9BYF1}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15231706}.
CC -!- PTM: Proteolytic cleavage by ADAM17 generates a secreted form. Also
CC cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-781 probably inhibits
CC interaction with AP2M1 and enables interactions with proteins
CC containing SH2 domains. {ECO:0000250|UniProtKB:Q9BYF1}.
CC -!- MISCELLANEOUS: In contrast to its human and palm-civet orthologs, does
CC not interact with SARS-CoV spike glycoprotein.
CC -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
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DR EMBL; AY881244; AAW78017.1; -; mRNA.
DR RefSeq; NP_001012006.1; NM_001012006.1.
DR AlphaFoldDB; Q5EGZ1; -.
DR SMR; Q5EGZ1; -.
DR IntAct; Q5EGZ1; 4.
DR STRING; 10116.ENSRNOP00000047913; -.
DR BindingDB; Q5EGZ1; -.
DR ChEMBL; CHEMBL2311; -.
DR DrugCentral; Q5EGZ1; -.
DR MEROPS; M02.006; -.
DR GlyGen; Q5EGZ1; 9 sites.
DR SwissPalm; Q5EGZ1; -.
DR PaxDb; Q5EGZ1; -.
DR Ensembl; ENSRNOT00000080730; ENSRNOP00000070410; ENSRNOG00000031665.
DR GeneID; 302668; -.
DR KEGG; rno:302668; -.
DR UCSC; RGD:728890; rat.
DR CTD; 59272; -.
DR RGD; 728890; Ace2.
DR eggNOG; KOG3690; Eukaryota.
DR GeneTree; ENSGT00940000158077; -.
DR InParanoid; Q5EGZ1; -.
DR OrthoDB; 422699at2759; -.
DR PhylomeDB; Q5EGZ1; -.
DR BRENDA; 3.4.17.23; 5301.
DR Reactome; R-RNO-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR PRO; PR:Q5EGZ1; -.
DR Proteomes; UP000002494; Chromosome X.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0031526; C:brush border membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004180; F:carboxypeptidase activity; IDA:CACAO.
DR GO; GO:0004175; F:endopeptidase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; ISO:RGD.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:RGD.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; ISO:RGD.
DR GO; GO:0001618; F:virus receptor activity; ISS:UniProtKB.
DR GO; GO:0003051; P:angiotensin-mediated drinking behavior; ISO:RGD.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:2000272; P:negative regulation of signaling receptor activity; ISO:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0051957; P:positive regulation of amino acid transport; ISO:RGD.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISO:RGD.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; ISO:RGD.
DR GO; GO:1905737; P:positive regulation of L-proline import across plasma membrane; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; ISO:RGD.
DR GO; GO:1903779; P:regulation of cardiac conduction; ISO:RGD.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; ISO:RGD.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015827; P:tryptophan transport; ISO:RGD.
DR GO; GO:0046718; P:viral entry into host cell; ISO:RGD.
DR CDD; cd06461; M2_ACE; 1.
DR InterPro; IPR031588; Collectrin_dom.
DR InterPro; IPR001548; Peptidase_M2.
DR PANTHER; PTHR10514; PTHR10514; 1.
DR Pfam; PF16959; Collectrin; 1.
DR Pfam; PF01401; Peptidase_M2; 1.
DR PRINTS; PR00791; PEPDIPTASEA.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell membrane; Cell projection; Chloride; Cytoplasm;
KW Disulfide bond; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome; Secreted;
KW Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..805
FT /note="Angiotensin-converting enzyme 2"
FT /id="PRO_0000028574"
FT CHAIN 18..708
FT /note="Processed angiotensin-converting enzyme 2"
FT /id="PRO_0000292272"
FT TOPO_DOM 18..740
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 652..659
FT /note="Essential for cleavage by ADAM17"
FT /evidence="ECO:0000250"
FT REGION 697..716
FT /note="Essential for cleavage by TMPRSS11D and TMPRSS2"
FT /evidence="ECO:0000250"
FT REGION 771..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 778..786
FT /note="LIR"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOTIF 781..785
FT /note="SH2-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOTIF 781..784
FT /note="Endocytic sorting signal"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOTIF 792..795
FT /note="PTB"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOTIF 803..805
FT /note="PDZ-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT COMPBIAS 790..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 169
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 345..346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 477
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 481
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOD_RES 781
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYF1"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 133..141
FT /evidence="ECO:0000250"
FT DISULFID 344..361
FT /evidence="ECO:0000250"
FT DISULFID 530..542
FT /evidence="ECO:0000250"
SQ SEQUENCE 805 AA; 92491 MW; A4079F2407960D28 CRC64;
MSSSCWLLLS LVAVATAQSL IEEKAESFLN KFNQEAEDLS YQSSLASWNY NTNITEENAQ
KMNEAAAKWS AFYEEQSKIA QNFSLQEIQN ATIKRQLKAL QQSGSSALSP DKNKQLNTIL
NTMSTIYSTG KVCNSMNPQE CFLLEPGLDE IMATSTDYNR RLWAWEGWRA EVGKQLRPLY
EEYVVLKNEM ARANNYEDYG DYWRGDYEAE GVEGYNYNRN QLIEDVENTF KEIKPLYEQL
HAYVRTKLME VYPSYISPTG CLPAHLLGDM WGRFWTNLYP LTTPFLQKPN IDVTDAMVNQ
SWDAERIFKE AEKFFVSVGL PQMTPGFWTN SMLTEPGDDR KVVCHPTAWD LGHGDFRIKM
CTKVTMDNFL TAHHEMGHIQ YDMAYAKQPF LLRNGANEGF HEAVGEIMSL SAATPKHLKS
IGLLPSNFQE DNETEINFLL KQALTIVGTL PFTYMLEKWR WMVFQDKIPR EQWTKKWWEM
KREIVGVVEP LPHDETYCDP ASLFHVSNDY SFIRYYTRTI YQFQFQEALC QAAKHDGPLH
KCDISNSTEA GQKLLNMLSL GNSGPWTLAL ENVVGSRNMD VKPLLNYFQP LFVWLKEQNR
NSTVGWSTDW SPYADQSIKV RISLKSALGK NAYEWTDNEM YLFRSSVAYA MREYFSREKN
QTVPFGEADV WVSDLKPRVS FNFFVTSPKN VSDIIPRSEV EEAIRMSRGR INDIFGLNDN
SLEFLGIYPT LKPPYEPPVT IWLIIFGVVM GTVVVGIVIL IVTGIKGRKK KNETKREENP
YDSMDIGKGE SNAGFQNSDD AQTSF