CCR3_HUMAN
ID CCR3_HUMAN Reviewed; 355 AA.
AC P51677; B3KVQ1; F5GWL6; Q15748; Q2YDB9; Q86WD2; Q8TDP6; Q9ULY8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=C-C chemokine receptor type 3;
DE Short=C C CKR3 {ECO:0000303|PubMed:7622448};
DE Short=C-C CKR-3;
DE Short=CC-CKR-3;
DE Short=CCR-3;
DE Short=CCR3;
DE Short=CKR 3 {ECO:0000303|PubMed:8676064};
DE Short=CKR3;
DE AltName: Full=Eosinophil eotaxin receptor;
DE AltName: CD_antigen=CD193;
GN Name=CCR3; Synonyms=CMKBR3;
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] (ISOFORM 1), FUNCTION, AND LIGAND-BINDING.
RC TISSUE=Monocyte;
RX PubMed=7622448; DOI=10.1074/jbc.270.28.16491;
RA Combadiere C., Ahuja S.K., Murphy P.M.;
RT "Cloning and functional expression of a human eosinophil CC chemokine
RT receptor.";
RL J. Biol. Chem. 270:16491-16494(1995).
RN [2]
RP ERRATUM OF PUBMED:7622448.
RA Combadiere C., Ahuja S.K., Murphy P.M.;
RL J. Biol. Chem. 270:30235-30235(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, AND
RP LIGAND-BINDING.
RX PubMed=8642344; DOI=10.1084/jem.183.5.2349;
RA Daugherty B.L., Siciliano S.J., Demartino J.A., Malkowitz L., Sirotina A.,
RA Springer M.S.;
RT "Cloning, expression, and characterization of the human eosinophil eotaxin
RT receptor.";
RL J. Exp. Med. 183:2349-2354(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP FUNCTION, AND LIGAND-BINDING.
RX PubMed=8676064; DOI=10.1084/jem.183.6.2437;
RA Ponath P.D., Qin S., Post T.W., Wang J., Wu L., Gerard N.P., Newman W.,
RA Gerard C., Mackay C.R.;
RT "Molecular cloning and characterization of a human eotaxin receptor
RT expressed selectively on eosinophils.";
RL J. Exp. Med. 183:2437-2448(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Xiao L., Weiss S., Qari S., Rudolph D., Hodge T., Lal R.;
RT "Partial resistance to infection by syncytium-inducing primary HIV-1 in
RT exposed uninfected individuals homozygous for CCR5 32bp deletion.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT SER-218.
RX PubMed=11196669; DOI=10.1038/sj.gene.6363638;
RA Kato H., Tsuchiya N., Izumi S., Miyamasu M., Nakajima T., Kawasaki H.,
RA Hirai K., Tokunaga K.;
RT "New variations of human CC-chemokine receptors CCR3 and CCR4.";
RL Genes Immun. 1:97-104(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=12079287; DOI=10.1006/geno.2002.6801;
RA Vijh S., Dayhoff D.E., Wang C.E., Imam Z., Ehrenberg P.K., Michael N.L.;
RT "Transcription regulation of human chemokine receptor CCR3: evidence for a
RT rare TATA-less promoter structure conserved between Drosophila and
RT humans.";
RL Genomics 80:86-95(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood;
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 [13]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=9789057; DOI=10.1073/pnas.95.22.13153;
RA Albini A., Ferrini S., Benelli R., Sforzini S., Giunciuglio D.,
RA Aluigi M.G., Proudfoot A.E.I., Alouani S., Wells T.N.C., Mariani G.,
RA Rabin R.L., Farber J.M., Noonan D.M.;
RT "HIV-1 Tat protein mimicry of chemokines.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:13153-13158(1998).
RN [14]
RP OVEREXPRESSION.
RX PubMed=21077277; DOI=10.1111/j.1365-2249.2010.04248.x;
RA Manousou P., Kolios G., Valatas V., Drygiannakis I., Bourikas L.,
RA Pyrovolaki K., Koutroubakis I., Papadaki H.A., Kouroumalis E.;
RT "Increased expression of chemokine receptor CCR3 and its ligands in
RT ulcerative colitis: the role of colonic epithelial cells in in vitro
RT studies.";
RL Clin. Exp. Immunol. 162:337-347(2010).
RN [15]
RP LIGAND-BINDING, AND FUNCTION.
RX PubMed=30171954; DOI=10.1016/j.ijbiomac.2018.08.171;
RA Park J.S., Park M.C., Lee K.Y., Goughnour P.C., Jeong S.J., Kim H.S.,
RA Kim H.J., Lee B.J., Kim S., Han B.W.;
RT "Unique N-terminal extension domain of human asparaginyl-tRNA synthetase
RT elicits CCR3-mediated chemokine activity.";
RL Int. J. Biol. Macromol. 120:835-845(2018).
CC -!- FUNCTION: Receptor for C-C type chemokine. Binds and responds to a
CC variety of chemokines, including CCL11, CCL26, CCL7, CCL13,
CC RANTES(CCL5) and CCL15 (PubMed:7622448, PubMed:8642344,
CC PubMed:8676064). Subsequently transduces a signal by increasing the
CC intracellular calcium ions level (PubMed:8676064). In addition acts as
CC a possible functional receptor for NARS1 (PubMed:30171954).
CC {ECO:0000269|PubMed:30171954, ECO:0000269|PubMed:7622448,
CC ECO:0000269|PubMed:8642344, ECO:0000269|PubMed:8676064}.
CC -!- FUNCTION: (Microbial infection) Alternative coreceptor with CD4 for
CC HIV-1 infection. {ECO:0000269|PubMed:9789057}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 protein Tat.
CC {ECO:0000269|PubMed:9789057}.
CC -!- INTERACTION:
CC P51677; P51671: CCL11; NbExp=2; IntAct=EBI-6625120, EBI-727357;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51677-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51677-2; Sequence=VSP_046704;
CC -!- TISSUE SPECIFICITY: In eosinophils as well as trace amounts in
CC neutrophils and monocytes. {ECO:0000269|PubMed:8676064}.
CC -!- MISCELLANEOUS: Overexpression of CCR3 together with its ligands appears
CC to be a characteristic of ulcerative colitis (UC). The production of
CC CCR3 ligands by human colonic epithelial cells suggests further that
CC the epithelium can play a role in modulating pathological T-cell-
CC mediated mucosal inflammation (PubMed:21077277).
CC {ECO:0000305|PubMed:21077277}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CC chemokine receptors entry;
CC URL="https://en.wikipedia.org/wiki/CC_chemokine_receptors";
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DR EMBL; U28694; AAC50469.1; -; mRNA.
DR EMBL; U51241; AAB16831.1; -; Genomic_DNA.
DR EMBL; U49727; AAB09726.1; -; Genomic_DNA.
DR EMBL; AF026535; AAB82589.1; -; mRNA.
DR EMBL; AB023887; BAA86964.1; -; Genomic_DNA.
DR EMBL; AF262301; AAL85630.1; -; mRNA.
DR EMBL; AF247361; AAL85154.1; -; Genomic_DNA.
DR EMBL; AY221092; AAO65970.2; -; Genomic_DNA.
DR EMBL; EF064760; ABK41943.1; -; Genomic_DNA.
DR EMBL; AK123050; BAG53863.1; -; mRNA.
DR EMBL; AC104439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110297; AAI10298.1; -; mRNA.
DR EMBL; BC130318; AAI30319.1; -; mRNA.
DR EMBL; BC130320; AAI30321.1; -; mRNA.
DR CCDS; CCDS2738.1; -. [P51677-1]
DR CCDS; CCDS54574.1; -. [P51677-2]
DR PIR; G02436; G02436.
DR RefSeq; NP_001828.1; NM_001837.3. [P51677-1]
DR RefSeq; NP_847898.1; NM_178328.1. [P51677-2]
DR RefSeq; NP_847899.1; NM_178329.2. [P51677-1]
DR RefSeq; XP_006713023.1; XM_006712960.3. [P51677-1]
DR RefSeq; XP_011531637.1; XM_011533335.2. [P51677-1]
DR AlphaFoldDB; P51677; -.
DR SMR; P51677; -.
DR BioGRID; 107637; 14.
DR DIP; DIP-5846N; -.
DR IntAct; P51677; 1.
DR STRING; 9606.ENSP00000441600; -.
DR BindingDB; P51677; -.
DR ChEMBL; CHEMBL3473; -.
DR GuidetoPHARMACOLOGY; 60; -.
DR GlyGen; P51677; 2 sites, 1 O-linked glycan (2 sites).
DR PhosphoSitePlus; P51677; -.
DR BioMuta; CCR3; -.
DR DMDM; 1705892; -.
DR PaxDb; P51677; -.
DR PeptideAtlas; P51677; -.
DR PRIDE; P51677; -.
DR ProteomicsDB; 24154; -.
DR ProteomicsDB; 56365; -. [P51677-1]
DR ABCD; P51677; 1 sequenced antibody.
DR Antibodypedia; 3532; 848 antibodies from 42 providers.
DR DNASU; 1232; -.
DR Ensembl; ENST00000357422.2; ENSP00000350003.2; ENSG00000183625.16. [P51677-1]
DR Ensembl; ENST00000395940.3; ENSP00000379271.2; ENSG00000183625.16. [P51677-1]
DR Ensembl; ENST00000395942.2; ENSP00000379273.2; ENSG00000183625.16. [P51677-1]
DR Ensembl; ENST00000545097.1; ENSP00000441600.1; ENSG00000183625.16. [P51677-2]
DR GeneID; 1232; -.
DR KEGG; hsa:1232; -.
DR MANE-Select; ENST00000395940.3; ENSP00000379271.2; NM_178329.3; NP_847899.1.
DR UCSC; uc003cpg.3; human. [P51677-1]
DR CTD; 1232; -.
DR DisGeNET; 1232; -.
DR GeneCards; CCR3; -.
DR HGNC; HGNC:1604; CCR3.
DR HPA; ENSG00000183625; Tissue enhanced (intestine).
DR MIM; 601268; gene.
DR neXtProt; NX_P51677; -.
DR OpenTargets; ENSG00000183625; -.
DR PharmGKB; PA26168; -.
DR VEuPathDB; HostDB:ENSG00000183625; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P51677; -.
DR OMA; DMGLLCE; -.
DR OrthoDB; 900867at2759; -.
DR PhylomeDB; P51677; -.
DR TreeFam; TF330966; -.
DR PathwayCommons; P51677; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P51677; -.
DR SIGNOR; P51677; -.
DR BioGRID-ORCS; 1232; 6 hits in 1061 CRISPR screens.
DR ChiTaRS; CCR3; human.
DR GenomeRNAi; 1232; -.
DR Pharos; P51677; Tchem.
DR PRO; PR:P51677; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P51677; protein.
DR Bgee; ENSG00000183625; Expressed in secondary oocyte and 71 other tissues.
DR ExpressionAtlas; P51677; baseline and differential.
DR Genevisible; P51677; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0019957; F:C-C chemokine binding; IDA:CAFA.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0006968; P:cellular defense response; TAS:ProtInc.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR InterPro; IPR002238; Chemokine_CCR3.
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; PR01108; CHEMOKINER3.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Host-virus interaction; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..355
FT /note="C-C chemokine receptor type 3"
FT /id="PRO_0000069239"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..171
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..203
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..264
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..355
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DISULFID 106..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1
FT /note="M -> MPFGIRMLLRAHKPGSSRRSEM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046704"
FT VARIANT 21
FT /note="G -> D (in dbSNP:rs4987125)"
FT /id="VAR_020067"
FT VARIANT 39
FT /note="P -> L (in dbSNP:rs5742906)"
FT /id="VAR_049382"
FT VARIANT 218
FT /note="C -> S"
FT /evidence="ECO:0000269|PubMed:11196669"
FT /id="VAR_010668"
FT CONFLICT 81..82
FT /note="LL -> QG (in Ref. 7; AAL85630)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="I -> V (in Ref. 10; BAG53863)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="S -> T (in Ref. 4; AAB09726 and 6; BAA86964)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="K -> R (in Ref. 10; BAG53863)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="P -> R (in Ref. 10; BAG53863)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 41044 MW; E95DCD7A6C643874 CRC64;
MTTSLDTVET FGTTSYYDDV GLLCEKADTR ALMAQFVPPL YSLVFTVGLL GNVVVVMILI
KYRRLRIMTN IYLLNLAISD LLFLVTLPFW IHYVRGHNWV FGHGMCKLLS GFYHTGLYSE
IFFIILLTID RYLAIVHAVF ALRARTVTFG VITSIVTWGL AVLAALPEFI FYETEELFEE
TLCSALYPED TVYSWRHFHT LRMTIFCLVL PLLVMAICYT GIIKTLLRCP SKKKYKAIRL
IFVIMAVFFI FWTPYNVAIL LSSYQSILFG NDCERSKHLD LVMLVTEVIA YSHCCMNPVI
YAFVGERFRK YLRHFFHRHL LMHLGRYIPF LPSEKLERTS SVSPSTAEPE LSIVF