AGRE1_HUMAN
ID AGRE1_HUMAN Reviewed; 886 AA.
AC Q14246; A6NHV2; B7Z486; B7Z489; E7EPX9; E9PD45; H9KV79; Q2I7G5; Q6ZMN0;
AC Q8NGA7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Adhesion G protein-coupled receptor E1 {ECO:0000303|PubMed:25713288};
DE AltName: Full=EGF-like module receptor 1;
DE AltName: Full=EGF-like module-containing mucin-like hormone receptor-like 1;
DE AltName: Full=EMR1 hormone receptor;
DE Flags: Precursor;
GN Name=ADGRE1 {ECO:0000312|HGNC:HGNC:3336}; Synonyms=EMR1, TM7LN3;
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), AND VARIANTS THR-57; ARG-140;
RP ASN-174; SER-254; VAL-298; MET-389; VAL-424; GLN-496; VAL-539 AND THR-663.
RX PubMed=7601460; DOI=10.1016/0888-7543(95)80218-b;
RA Baud V., Chissoe S.L., Viegas-Pequignot E., Diriong S., N'Guyen V.C.,
RA Roe B.A., Lipinski M.;
RT "EMR1, an unusual member in the family of hormone receptors with seven
RT transmembrane segments.";
RL Genomics 26:334-344(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-424; GLN-496 AND
RP VAL-539.
RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT "Genome-wide discovery and analysis of human seven transmembrane helix
RT receptor genes.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tan J., Davila S., Hibberd M.L., Seielstad M.;
RT "Genetic variation in EMR1 gene.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5), AND VARIANTS
RP THR-57; VAL-424; GLN-496; VAL-539 AND ILE-589.
RC TISSUE=Thymus, and Umbilical cord blood;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-589.
RC TISSUE=Placenta;
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=17823986; DOI=10.1002/eji.200737553;
RA Hamann J., Koning N., Pouwels W., Ulfman L.H., van Eijk M., Stacey M.,
RA Lin H.H., Gordon S., Kwakkenbos M.J.;
RT "EMR1, the human homolog of F4/80, is an eosinophil-specific receptor.";
RL Eur. J. Immunol. 37:2797-2802(2007).
RN [8]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=24530099; DOI=10.1016/j.jaci.2013.11.041;
RA Legrand F., Tomasevic N., Simakova O., Lee C.C., Wang Z., Raffeld M.,
RA Makiya M.A., Palath V., Leung J., Baer M., Yarranton G., Maric I.,
RA Bebbington C., Klion A.D.;
RT "The eosinophil surface receptor epidermal growth factor-like module
RT containing mucin-like hormone receptor 1 (EMR1): a novel therapeutic target
RT for eosinophilic disorders.";
RL J. Allergy Clin. Immunol. 133:1439-1447(2014).
RN [9]
RP NOMENCLATURE.
RX PubMed=25713288; DOI=10.1124/pr.114.009647;
RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT protein-coupled receptors.";
RL Pharmacol. Rev. 67:338-367(2015).
CC -!- FUNCTION: Orphan receptor involved in cell adhesion and probably in
CC cell-cell interactions specifically involving cells of the immune
CC system. May play a role in regulatory T-cells (Treg) development.
CC {ECO:0000250|UniProtKB:Q61549}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24530099};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q14246-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14246-2; Sequence=VSP_009594;
CC Name=3;
CC IsoId=Q14246-3; Sequence=VSP_045521, VSP_045524;
CC Name=4;
CC IsoId=Q14246-4; Sequence=VSP_045523;
CC Name=5;
CC IsoId=Q14246-5; Sequence=VSP_045521, VSP_045522;
CC -!- TISSUE SPECIFICITY: Expression is restricted to eosinophils.
CC {ECO:0000269|PubMed:17823986, ECO:0000269|PubMed:24530099}.
CC -!- MISCELLANEOUS: Most adhesion GPCRs proteins undergo autoproteolysis at
CC the GPS domain. ADGRE1 is predicted non-cleavable because of the lack
CC of a consensus catalytic triad sequence within GPS domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC06133.1; Type=Erroneous gene model prediction; Evidence={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; X81479; CAA57232.1; -; mRNA.
DR EMBL; AB065918; BAC06133.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DQ217942; ABB70739.1; -; Genomic_DNA.
DR EMBL; AK131562; BAD18695.1; -; mRNA.
DR EMBL; AK297003; BAH12472.1; -; mRNA.
DR EMBL; AK297011; BAH12475.1; -; mRNA.
DR EMBL; AC020895; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059395; AAH59395.1; -; mRNA.
DR CCDS; CCDS12175.1; -. [Q14246-1]
DR CCDS; CCDS58643.1; -. [Q14246-4]
DR CCDS; CCDS58644.1; -. [Q14246-2]
DR CCDS; CCDS58645.1; -. [Q14246-3]
DR CCDS; CCDS58646.1; -. [Q14246-5]
DR PIR; A57172; A57172.
DR RefSeq; NP_001243181.1; NM_001256252.1. [Q14246-3]
DR RefSeq; NP_001243182.1; NM_001256253.1. [Q14246-2]
DR RefSeq; NP_001243183.1; NM_001256254.1. [Q14246-5]
DR RefSeq; NP_001243184.1; NM_001256255.1. [Q14246-4]
DR RefSeq; NP_001965.3; NM_001974.4. [Q14246-1]
DR AlphaFoldDB; Q14246; -.
DR IntAct; Q14246; 1.
DR STRING; 9606.ENSP00000311545; -.
DR TCDB; 9.A.14.6.1; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q14246; 12 sites.
DR iPTMnet; Q14246; -.
DR PhosphoSitePlus; Q14246; -.
DR BioMuta; ADGRE1; -.
DR DMDM; 290457673; -.
DR MassIVE; Q14246; -.
DR PaxDb; Q14246; -.
DR PeptideAtlas; Q14246; -.
DR PRIDE; Q14246; -.
DR ProteomicsDB; 17463; -.
DR ProteomicsDB; 19583; -.
DR ProteomicsDB; 46230; -.
DR ProteomicsDB; 59945; -. [Q14246-1]
DR ProteomicsDB; 59946; -. [Q14246-2]
DR ABCD; Q14246; 11 sequenced antibodies.
DR Antibodypedia; 11973; 715 antibodies from 41 providers.
DR DNASU; 2015; -.
DR Ensembl; ENST00000250572.12; ENSP00000250572.7; ENSG00000174837.15. [Q14246-2]
DR Ensembl; ENST00000312053.9; ENSP00000311545.3; ENSG00000174837.15. [Q14246-1]
DR Ensembl; ENST00000381404.8; ENSP00000370811.4; ENSG00000174837.15. [Q14246-3]
DR Ensembl; ENST00000381407.9; ENSP00000370814.4; ENSG00000174837.15. [Q14246-5]
DR Ensembl; ENST00000450315.7; ENSP00000405974.2; ENSG00000174837.15. [Q14246-4]
DR GeneID; 2015; -.
DR KEGG; hsa:2015; -.
DR MANE-Select; ENST00000312053.9; ENSP00000311545.3; NM_001974.5; NP_001965.3.
DR UCSC; uc002mfw.5; human. [Q14246-1]
DR CTD; 2015; -.
DR DisGeNET; 2015; -.
DR GeneCards; ADGRE1; -.
DR HGNC; HGNC:3336; ADGRE1.
DR HPA; ENSG00000174837; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 600493; gene.
DR neXtProt; NX_Q14246; -.
DR OpenTargets; ENSG00000174837; -.
DR PharmGKB; PA27773; -.
DR VEuPathDB; HostDB:ENSG00000174837; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000161354; -.
DR HOGENOM; CLU_002753_3_7_1; -.
DR InParanoid; Q14246; -.
DR OMA; PGRFICT; -.
DR OrthoDB; 124090at2759; -.
DR PhylomeDB; Q14246; -.
DR TreeFam; TF316380; -.
DR PathwayCommons; Q14246; -.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR SignaLink; Q14246; -.
DR BioGRID-ORCS; 2015; 9 hits in 1069 CRISPR screens.
DR ChiTaRS; ADGRE1; human.
DR GeneWiki; EMR1; -.
DR GenomeRNAi; 2015; -.
DR Pharos; Q14246; Tbio.
DR PRO; PR:Q14246; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q14246; protein.
DR Bgee; ENSG00000174837; Expressed in monocyte and 103 other tissues.
DR ExpressionAtlas; Q14246; baseline and differential.
DR Genevisible; Q14246; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR001740; GPCR_2_EMR1-like_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 4.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR01128; EMR1HORMONER.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 5.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Alternative splicing; Calcium; Cell membrane;
KW Disulfide bond; EGF-like domain; G-protein coupled receptor; Glycoprotein;
KW Immunity; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..886
FT /note="Adhesion G protein-coupled receptor E1"
FT /id="PRO_0000012873"
FT TOPO_DOM 21..599
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 600..627
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 635..656
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..666
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 667..690
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 691..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 710..731
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..747
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 748..776
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..794
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 795..814
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 815..829
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 830..852
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 853..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 31..79
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 80..131
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 132..171
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 172..220
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 221..267
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 268..316
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 547..596
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 862..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 41..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 58..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 84..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 91..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 108..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 136..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 142..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 159..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 176..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 182..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 199..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 225..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 229..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 246..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 272..285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 279..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 296..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 80..131
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045521"
FT VAR_SEQ 132..220
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045522"
FT VAR_SEQ 140..316
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045523"
FT VAR_SEQ 599..663
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009594"
FT VAR_SEQ 764
FT /note="I -> VSKYYNSLAKCVLKEEQGDLRDLEFPGTCAAERI (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045524"
FT VARIANT 2
FT /note="R -> L (in dbSNP:rs34176643)"
FT /id="VAR_046976"
FT VARIANT 57
FT /note="A -> T (in dbSNP:rs330877)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7601460"
FT /id="VAR_027616"
FT VARIANT 140
FT /note="S -> R (in dbSNP:rs330880)"
FT /evidence="ECO:0000269|PubMed:7601460"
FT /id="VAR_027617"
FT VARIANT 174
FT /note="D -> N (in dbSNP:rs897738)"
FT /evidence="ECO:0000269|PubMed:7601460"
FT /id="VAR_027618"
FT VARIANT 254
FT /note="N -> S (in dbSNP:rs443658)"
FT /evidence="ECO:0000269|PubMed:7601460"
FT /id="VAR_027619"
FT VARIANT 298
FT /note="A -> V (in dbSNP:rs370094)"
FT /evidence="ECO:0000269|PubMed:7601460"
FT /id="VAR_027620"
FT VARIANT 389
FT /note="T -> M (in dbSNP:rs466876)"
FT /evidence="ECO:0000269|PubMed:7601460"
FT /id="VAR_027621"
FT VARIANT 424
FT /note="I -> V (in dbSNP:rs457857)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7601460, ECO:0000269|Ref.2"
FT /id="VAR_027622"
FT VARIANT 496
FT /note="K -> Q (in dbSNP:rs373533)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7601460, ECO:0000269|Ref.2"
FT /id="VAR_027623"
FT VARIANT 539
FT /note="I -> V (in dbSNP:rs461645)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7601460, ECO:0000269|Ref.2"
FT /id="VAR_027624"
FT VARIANT 589
FT /note="V -> I (in dbSNP:rs7256147)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_027625"
FT VARIANT 663
FT /note="M -> T (in dbSNP:rs2228539)"
FT /evidence="ECO:0000269|PubMed:7601460"
FT /id="VAR_046977"
FT VARIANT 691
FT /note="F -> C (in dbSNP:rs2229769)"
FT /id="VAR_027626"
FT VARIANT 724
FT /note="V -> L (in dbSNP:rs10406580)"
FT /id="VAR_027627"
FT CONFLICT 61
FT /note="G -> R (in Ref. 4; BAH12472)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="F -> C (in Ref. 1; CAA57232)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="I -> A (in Ref. 4; BAH12475)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="T -> A (in Ref. 1; CAA57232)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="F -> L (in Ref. 4; BAH12475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 886 AA; 97683 MW; 07322996EEF5A6F1 CRC64;
MRGFNLLLFW GCCVMHSWEG HIRPTRKPNT KGNNCRDSTL CPAYATCTNT VDSYYCACKQ
GFLSSNGQNH FKDPGVRCKD IDECSQSPQP CGPNSSCKNL SGRYKCSCLD GFSSPTGNDW
VPGKPGNFSC TDINECLTSS VCPEHSDCVN SMGSYSCSCQ VGFISRNSTC EDVDECADPR
ACPEHATCNN TVGNYSCFCN PGFESSSGHL SFQGLKASCE DIDECTEMCP INSTCTNTPG
SYFCTCHPGF APSNGQLNFT DQGVECRDID ECRQDPSTCG PNSICTNALG SYSCGCIAGF
HPNPEGSQKD GNFSCQRVLF KCKEDVIPDN KQIQQCQEGT AVKPAYVSFC AQINNIFSVL
DKVCENKTTV VSLKNTTESF VPVLKQISTW TKFTKEETSS LATVFLESVE SMTLASFWKP
SANITPAVRT EYLDIESKVI NKECSEENVT LDLVAKGDKM KIGCSTIEES ESTETTGVAF
VSFVGMESVL NERFFKDHQA PLTTSEIKLK MNSRVVGGIM TGEKKDGFSD PIIYTLENIQ
PKQKFERPIC VSWSTDVKGG RWTSFGCVIL EASETYTICS CNQMANLAVI MASGELTMDF
SLYIISHVGI IISLVCLVLA IATFLLCRSI RNHNTYLHLH LCVCLLLAKT LFLAGIHKTD
NKMGCAIIAG FLHYLFLACF FWMLVEAVIL FLMVRNLKVV NYFSSRNIKM LHICAFGYGL
PMLVVVISAS VQPQGYGMHN RCWLNTETGF IWSFLGPVCT VIVINSLLLT WTLWILRQRL
SSVNAEVSTL KDTRLLTFKA FAQLFILGCS WVLGIFQIGP VAGVMAYLFT IINSLQGAFI
FLIHCLLNGQ VREEYKRWIT GKTKPSSQSQ TSRILLSSMP SASKTG
