CCR2_MOUSE
ID CCR2_MOUSE Reviewed; 373 AA.
AC P51683; Q61172;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=C-C chemokine receptor type 2;
DE Short=C-C CKR-2;
DE Short=CC-CKR-2;
DE Short=CCR-2;
DE Short=CCR2;
DE AltName: Full=JE/FIC receptor;
DE AltName: Full=MCP-1 receptor;
DE AltName: CD_antigen=CD192;
GN Name=Ccr2; Synonyms=Cmkbr2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8631787; DOI=10.1074/jbc.271.13.7551;
RA Boring L., Gosling J., Monteclaro F.S., Lusis A.J., Tsou C.-L., Charo I.F.;
RT "Molecular cloning and functional expression of murine JE (monocyte
RT chemoattractant protein 1) and murine macrophage inflammatory protein
RT 1alpha receptors: evidence for two closely linked C-C chemokine receptors
RT on chromosome 9.";
RL J. Biol. Chem. 271:7551-7558(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=BALB/cJ;
RX PubMed=8662823; DOI=10.1074/jbc.271.20.11603;
RA Kurihara T., Bravo R.;
RT "Cloning and functional expression of mCCR2, a murine receptor for the C-C
RT chemokines JE and FIC.";
RL J. Biol. Chem. 271:11603-11606(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8872898;
RX DOI=10.1002/(sici)1097-4547(19960815)45:4<382::aid-jnr7>3.0.co;2-5;
RA Heesen M., Tanabe S., Berman M.A., Yoshizawa I., Luo Y., Kim R., Post T.W.,
RA Gerard C., Dorf M.E.;
RT "Mouse astrocytes respond to the chemokines MCP-1 and KC, but reverse
RT transcriptase-polymerase chain reaction does not detect mRNA for the KC or
RT new MCP-1 receptor.";
RL J. Neurosci. Res. 45:382-391(1996).
RN [4]
RP FUNCTION AS CCL12 RECEPTOR, AND SUBCELLULAR LOCATION.
RX PubMed=8996246; DOI=10.1084/jem.185.1.99;
RA Sarafi M.N., Garcia-Zepeda E.A., MacLean J.A., Charo I.F., Luster A.D.;
RT "Murine monocyte chemoattractant protein (MCP)-5: a novel CC chemokine that
RT is a structural and functional homologue of human MCP-1.";
RL J. Exp. Med. 185:99-109(1997).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24806994; DOI=10.1089/neu.2013.3252;
RA Hsieh C.L., Niemi E.C., Wang S.H., Lee C.C., Bingham D., Zhang J.,
RA Cozen M.L., Charo I., Huang E.J., Liu J., Nakamura M.C.;
RT "CCR2 deficiency impairs macrophage infiltration and improves cognitive
RT function after traumatic brain injury.";
RL J. Neurotrauma 31:1677-1688(2014).
RN [6]
RP FUNCTION.
RX PubMed=28507030; DOI=10.4049/jimmunol.1601458;
RA Bakos E., Thaiss C.A., Kramer M.P., Cohen S., Radomir L., Orr I.,
RA Kaushansky N., Ben-Nun A., Becker-Herman S., Shachar I.;
RT "CCR2 regulates the immune response by modulating the interconversion and
RT function of effector and regulatory T cells.";
RL J. Immunol. 198:4659-4671(2017).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29632244; DOI=10.15252/embr.201745294;
RA Frik J., Merl-Pham J., Plesnila N., Mattugini N., Kjell J., Kraska J.,
RA Gomez R.M., Hauck S.M., Sirko S., Goetz M.;
RT "Cross-talk between monocyte invasion and astrocyte proliferation regulates
RT scarring in brain injury.";
RL EMBO Rep. 19:0-0(2018).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=29930553; DOI=10.3389/fimmu.2018.01263;
RA Aili A., Zhang J., Wu J., Wu H., Sun X., He Q., Jin R., Zhang Y.;
RT "CCR2 signal facilitates thymic egress by priming thymocyte responses to
RT sphingosine-1-phosphate.";
RL Front. Immunol. 9:1263-1263(2018).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=29993042; DOI=10.1038/s41386-018-0115-8;
RA Wu X.B., Jing P.B., Zhang Z.J., Cao D.L., Gao M.H., Jiang B.C., Gao Y.J.;
RT "Chemokine receptor CCR2 contributes to neuropathic pain and the associated
RT depression via increasing NR2B-mediated currents in both D1 and D2 dopamine
RT receptor-containing medium spiny neurons in the nucleus accumbens shell.";
RL Neuropsychopharmacology 43:2320-2330(2018).
CC -!- FUNCTION: Key functional receptor for CCL2 but can also bind CCL7 and
CC CCL12 chemokines (PubMed:8631787, PubMed:8662823, PubMed:8996246). Its
CC binding with CCL2 on monocytes and macrophages mediates chemotaxis and
CC migration induction through the activation of the PI3K cascade, the
CC small G protein Rac and lamellipodium protrusion (By similarity). Also
CC acts as a receptor for the beta-defensin DEFB106A/DEFB106B (By
CC similarity). Regulates the expression of T-cell inflammatory cytokines
CC and T-cell differentiation, promoting the differentiation of T-cells
CC into T-helper 17 cells (Th17) during inflammation (PubMed:28507030).
CC Facilitates the export of mature thymocytes by enhancing directional
CC movement of thymocytes to sphingosine-1-phosphate stimulation and up-
CC regulation of S1P1R expression; signals through the JAK-STAT pathway to
CC regulate FOXO1 activity leading to an increased expression of S1P1R
CC (PubMed:29930553). Plays an important role in mediating peripheral
CC nerve injury-induced neuropathic pain (PubMed:29993042). Increases
CC NMDA-mediated synaptic transmission in both dopamine D1 and D2
CC receptor-containing neurons, which may be caused by MAPK/ERK-dependent
CC phosphorylation of GRIN2B/NMDAR2B (PubMed:29993042). Mediates the
CC recruitment of macrophages and monocytes to the injury site following
CC brain injury (PubMed:24806994, PubMed:29632244).
CC {ECO:0000250|UniProtKB:P41597, ECO:0000269|PubMed:24806994,
CC ECO:0000269|PubMed:28507030, ECO:0000269|PubMed:29632244,
CC ECO:0000269|PubMed:29930553, ECO:0000269|PubMed:29993042,
CC ECO:0000269|PubMed:8631787, ECO:0000269|PubMed:8662823,
CC ECO:0000269|PubMed:8996246}.
CC -!- SUBUNIT: Interacts with ARRB1 (By similarity). Interacts (via
CC extracellular N-terminal region) with beta-defensin DEFB106A/DEFB106B;
CC this interaction may preferentially require specific tyrosine sulfation
CC on CCR2 (By similarity). Interacts with NUP85; the interaction is
CC required for CCR2 clusters formation on the cell membrane and CCR2
CC signaling (By similarity). {ECO:0000250|UniProtKB:P41597}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8996246};
CC Multi-pass membrane protein {ECO:0000255}. Note=The chemoattractant
CC receptors are reportedly distributed throughout the cell surface; after
CC stimulation with a ligand, such as CCL2, they are rapidly recruited
CC into microdomain clusters at the cell membrane.
CC {ECO:0000250|UniProtKB:P41597}.
CC -!- TISSUE SPECIFICITY: Epressed in mature thymocytes (PubMed:29930553).
CC Detected in monocyte/macrophage cell lines, but not in nonhematopoietic
CC cell lines (PubMed:8631787). {ECO:0000269|PubMed:29930553,
CC ECO:0000269|PubMed:8631787}.
CC -!- INDUCTION: Up-regulated in the dopamine D1 and D2 receptor-containing
CC neurons of nucleus accumbens shell after spinal nerve ligation.
CC {ECO:0000269|PubMed:29993042}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41597}.
CC -!- PTM: Sulfation increases the affinity for both monomeric and dimeric
CC CCL2 with stronger binding to the monomeric form (By similarity).
CC Binding of sulfated CCR2 to CCL2 promotes conversion of CCL2 from dimer
CC to monomer (By similarity). {ECO:0000250|UniProtKB:P41597}.
CC -!- DISRUPTION PHENOTYPE: Following a stab wound brain injury, mice show
CC reduced extracellular matrix deposition at the injured gray matter and
CC reduced astroglial scar in the cerebral cortex (PubMed:29632244). The
CC injury site shows an absence of invading monocytes, significantly
CC increased astrocyte proliferation and a decrease in extracellular
CC matrix synthesizing enzymes (PubMed:29632244). Following traumatic
CC brain injury, mice exhibit markedly reduced early macrophage
CC infiltration, improved locomotor activity, improved spatial learning
CC and memory retention and increased neuronal density in the CA1-CA3
CC regions of the hippocampus (PubMed:24806994). Mice show impaired thymic
CC emigration with a concomitant accumulation of mature thymocytes in the
CC thymus (PubMed:29930553). {ECO:0000269|PubMed:24806994,
CC ECO:0000269|PubMed:29632244, ECO:0000269|PubMed:29930553}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U47035; AAC52453.1; -; mRNA.
DR EMBL; U51717; AAC52557.1; -; mRNA.
DR EMBL; U56819; AAC52784.1; -; mRNA.
DR CCDS; CCDS23669.1; -.
DR RefSeq; NP_034045.1; NM_009915.2.
DR RefSeq; XP_006512491.1; XM_006512428.2.
DR RefSeq; XP_011241365.1; XM_011243063.1.
DR RefSeq; XP_011241366.1; XM_011243064.2.
DR AlphaFoldDB; P51683; -.
DR SMR; P51683; -.
DR BioGRID; 198772; 3.
DR STRING; 10090.ENSMUSP00000132453; -.
DR BindingDB; P51683; -.
DR ChEMBL; CHEMBL5412; -.
DR GuidetoPHARMACOLOGY; 59; -.
DR iPTMnet; P51683; -.
DR PhosphoSitePlus; P51683; -.
DR EPD; P51683; -.
DR PaxDb; P51683; -.
DR PRIDE; P51683; -.
DR ProteomicsDB; 281128; -.
DR Antibodypedia; 29661; 862 antibodies from 38 providers.
DR DNASU; 12772; -.
DR Ensembl; ENSMUST00000055918; ENSMUSP00000049909; ENSMUSG00000049103.
DR Ensembl; ENSMUST00000165984; ENSMUSP00000128734; ENSMUSG00000049103.
DR Ensembl; ENSMUST00000168841; ENSMUSP00000132453; ENSMUSG00000049103.
DR Ensembl; ENSMUST00000171719; ENSMUSP00000130112; ENSMUSG00000049103.
DR GeneID; 12772; -.
DR KEGG; mmu:12772; -.
DR UCSC; uc009shc.1; mouse.
DR CTD; 729230; -.
DR MGI; MGI:106185; Ccr2.
DR VEuPathDB; HostDB:ENSMUSG00000049103; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P51683; -.
DR OMA; ACAPYFP; -.
DR OrthoDB; 937138at2759; -.
DR PhylomeDB; P51683; -.
DR TreeFam; TF330966; -.
DR BioGRID-ORCS; 12772; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Ccr2; mouse.
DR PRO; PR:P51683; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P51683; protein.
DR Bgee; ENSMUSG00000049103; Expressed in lumbar dorsal root ganglion and 106 other tissues.
DR ExpressionAtlas; P51683; baseline and differential.
DR Genevisible; P51683; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0043204; C:perikaryon; ISS:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0150001; C:primary dendrite; ISO:MGI.
DR GO; GO:0019957; F:C-C chemokine binding; IBA:GO_Central.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IDA:MGI.
DR GO; GO:0035716; F:chemokine (C-C motif) ligand 12 binding; IPI:BHF-UCL.
DR GO; GO:0035715; F:chemokine (C-C motif) ligand 2 binding; IPI:BHF-UCL.
DR GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; IBA:GO_Central.
DR GO; GO:0035717; F:chemokine (C-C motif) ligand 7 binding; IPI:BHF-UCL.
DR GO; GO:0019955; F:cytokine binding; IPI:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; TAS:BHF-UCL.
DR GO; GO:0043277; P:apoptotic cell clearance; IC:BHF-UCL.
DR GO; GO:0001974; P:blood vessel remodeling; ISS:BHF-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:BHF-UCL.
DR GO; GO:0006968; P:cellular defense response; IMP:MGI.
DR GO; GO:0019725; P:cellular homeostasis; IDA:BHF-UCL.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0006959; P:humoral immune response; IMP:MGI.
DR GO; GO:0006955; P:immune response; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0090594; P:inflammatory response to wounding; IMP:UniProtKB.
DR GO; GO:0061756; P:leukocyte adhesion to vascular endothelial cell; IMP:MGI.
DR GO; GO:1905517; P:macrophage migration; IMP:UniProtKB.
DR GO; GO:0002548; P:monocyte chemotaxis; IMP:MGI.
DR GO; GO:0035696; P:monocyte extravasation; IMP:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0043310; P:negative regulation of eosinophil degranulation; IMP:BHF-UCL.
DR GO; GO:0002829; P:negative regulation of type 2 immune response; IMP:BHF-UCL.
DR GO; GO:0097350; P:neutrophil clearance; IMP:MGI.
DR GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IMP:BHF-UCL.
DR GO; GO:2000464; P:positive regulation of astrocyte chemotaxis; ISS:BHF-UCL.
DR GO; GO:2000451; P:positive regulation of CD8-positive, alpha-beta T cell extravasation; IMP:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; IMP:BHF-UCL.
DR GO; GO:0090265; P:positive regulation of immune complex clearance by monocytes and macrophages; IMP:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:BHF-UCL.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:BHF-UCL.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:BHF-UCL.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:MGI.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IMP:BHF-UCL.
DR GO; GO:2000439; P:positive regulation of monocyte extravasation; IMP:BHF-UCL.
DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; ISO:MGI.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:UniProtKB.
DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:BHF-UCL.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0045627; P:positive regulation of T-helper 1 cell differentiation; IC:BHF-UCL.
DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IMP:BHF-UCL.
DR GO; GO:2000412; P:positive regulation of thymocyte migration; IMP:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:BHF-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:1905521; P:regulation of macrophage migration; IMP:MGI.
DR GO; GO:0071675; P:regulation of mononuclear cell migration; IMP:MGI.
DR GO; GO:0002724; P:regulation of T cell cytokine production; IMP:UniProtKB.
DR GO; GO:0045580; P:regulation of T cell differentiation; IMP:UniProtKB.
DR GO; GO:2000404; P:regulation of T cell migration; IMP:MGI.
DR GO; GO:0010574; P:regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0035705; P:T-helper 17 cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0002246; P:wound healing involved in inflammatory response; NAS:BHF-UCL.
DR InterPro; IPR002237; Chemokine_CCR2.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR01107; CHEMOKINER2.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Inflammatory response; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..373
FT /note="C-C chemokine receptor type 2"
FT /id="PRO_0000069234"
FT TOPO_DOM 1..55
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..83
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..191
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..219
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..239
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..281
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 152
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000250|UniProtKB:P41597"
FT DISULFID 126..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 39
FT /note="Y -> H (in Ref. 1; AAC52453)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> G (in Ref. 1; AAC52453)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="V -> G (in Ref. 1; AAC52453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 42783 MW; FA012C10F4C9325A CRC64;
MEDNNMLPQF IHGILSTSHS LFTRSIQELD EGATTPYDYD DGEPCHKTSV KQIGAWILPP
LYSLVFIFGF VGNMLVIIIL IGCKKLKSMT DIYLLNLAIS DLLFLLTLPF WAHYAANEWV
FGNIMCKVFT GLYHIGYFGG IFFIILLTID RYLAIVHAVF ALKARTVTFG VITSVVTWVV
AVFASLPGII FTKSKQDDHH YTCGPYFTQL WKNFQTIMRN ILSLILPLLV MVICYSGILH
TLFRCRNEKK RHRAVRLIFA IMIVYFLFWT PYNIVLFLTT FQESLGMSNC VIDKHLDQAM
QVTETLGMTH CCINPVIYAF VGEKFRRYLS IFFRKHIAKR LCKQCPVFYR ETADRVSSTF
TPSTGEQEVS VGL
