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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
 
 
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