ACE2_FELCA
ID ACE2_FELCA Reviewed; 805 AA.
AC Q56H28; Q2PGE2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang C., Guo A.Z., Chen H.C.;
RT "Identification of cat ACE2 gene and its potential function as a SARS-CoV
RT receptor.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Zamoto A., Tagichi F., Fukushi S., Morikawa S., Yamada Y.K.;
RT "Identification of cat and racoon ACE2 and the its receptor function for
RT SARS-CoV.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- 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 -!- 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: 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 -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY957464; AAX59005.1; -; mRNA.
DR EMBL; AB211997; BAE72461.1; -; mRNA.
DR RefSeq; NP_001034545.1; NM_001039456.1.
DR RefSeq; XP_006943638.1; XM_006943576.2.
DR RefSeq; XP_019678890.1; XM_019823331.1.
DR PDB; 7C8D; EM; 3.00 A; A=18-740.
DR PDBsum; 7C8D; -.
DR AlphaFoldDB; Q56H28; -.
DR SMR; Q56H28; -.
DR BioGRID; 3230255; 1.
DR IntAct; Q56H28; 3.
DR STRING; 9685.ENSFCAP00000008647; -.
DR MEROPS; M02.006; -.
DR PRIDE; Q56H28; -.
DR Ensembl; ENSFCAT00000009326; ENSFCAP00000008647; ENSFCAG00000009320.
DR GeneID; 554349; -.
DR KEGG; fca:554349; -.
DR CTD; 59272; -.
DR VGNC; VGNC:59506; ACE2.
DR eggNOG; KOG3690; Eukaryota.
DR GeneTree; ENSGT00940000158077; -.
DR HOGENOM; CLU_014364_3_0_1; -.
DR InParanoid; Q56H28; -.
DR OMA; FTVIHHE; -.
DR OrthoDB; 422699at2759; -.
DR BRENDA; 3.4.17.23; 2235.
DR Proteomes; UP000011712; Chromosome X.
DR Bgee; ENSFCAG00000009320; Expressed in adult mammalian kidney and 7 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR GO; GO:0001618; F:virus receptor activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carboxypeptidase; Cell membrane; Cell projection; Chloride;
KW Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix;
KW Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..805
FT /note="Angiotensin-converting enzyme 2"
FT /id="PRO_0000028569"
FT CHAIN 18..708
FT /note="Processed angiotensin-converting enzyme 2"
FT /id="PRO_0000292267"
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 776..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 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
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 322
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 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"
FT HELIX 21..52
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 57..80
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:7C8D"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:7C8D"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:7C8D"
FT TURN 171..176
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 177..193
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:7C8D"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 221..251
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 367..384
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 401..412
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:7C8D"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 434..446
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 450..465
FT /evidence="ECO:0007829|PDB:7C8D"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 473..483
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 499..502
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 514..532
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 548..558
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 559..563
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 566..574
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 582..587
FT /evidence="ECO:0007829|PDB:7C8D"
FT HELIX 589..598
FT /evidence="ECO:0007829|PDB:7C8D"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:7C8D"
SQ SEQUENCE 805 AA; 92708 MW; 9F41A2EF300BE19E CRC64;
MSGSFWLLLS FAALTAAQST TEELAKTFLE KFNHEAEELS YQSSLASWNY NTNITDENVQ
KMNEAGAKWS AFYEEQSKLA KTYPLAEIHN TTVKRQLQAL QQSGSSVLSA DKSQRLNTIL
NAMSTIYSTG KACNPNNPQE CLLLEPGLDD IMENSKDYNE RLWAWEGWRA EVGKQLRPLY
EEYVALKNEM ARANNYEDYG DYWRGDYEEE WTDGYNYSRS QLIKDVEHTF TQIKPLYQHL
HAYVRAKLMD TYPSRISPTG CLPAHLLGDM WGRFWTNLYP LTVPFGQKPN IDVTDAMVNQ
SWDARRIFKE AEKFFVSVGL PNMTQGFWEN SMLTEPGDSR KVVCHPTAWD LGKGDFRIKM
CTKVTMDDFL TAHHEMGHIQ YDMAYAVQPF LLRNGANEGF HEAVGEIMSL SAATPNHLKT
IGLLSPGFSE DSETEINFLL KQALTIVGTL PFTYMLEKWR WMVFKGEIPK EQWMQKWWEM
KREIVGVVEP VPHDETYCDP ASLFHVANDY SFIRYYTRTI YQFQFQEALC RIAKHEGPLH
KCDISNSSEA GKKLLQMLTL GKSKPWTLAL EHVVGEKKMN VTPLLKYFEP LFTWLKEQNR
NSFVGWNTDW RPYADQSIKV RISLKSALGD EAYEWNDNEM YLFRSSVAYA MREYFSKVKN
QTIPFVEDNV WVSNLKPRIS FNFFVTASKN VSDVIPRSEV EEAIRMSRSR INDAFRLDDN
SLEFLGIQPT LSPPYQPPVT IWLIVFGVVM GVVVVGIVLL IVSGIRNRRK NNQARSEENP
YASVDLSKGE NNPGFQHADD VQTSF
