ACKR1_HUMAN
ID ACKR1_HUMAN Reviewed; 336 AA.
AC Q16570; A8YPG5; O75898; Q16300; Q8WWE3; Q9UJP0; Q9UKZ5; Q9UKZ6; Q9UQE1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Atypical chemokine receptor 1;
DE AltName: Full=Duffy antigen/chemokine receptor;
DE AltName: Full=Fy glycoprotein;
DE Short=GpFy;
DE AltName: Full=Glycoprotein D;
DE AltName: Full=Plasmodium vivax receptor;
DE AltName: CD_antigen=CD234;
GN Name=ACKR1; Synonyms=DARC, FY, GPD;
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), PARTIAL PROTEIN SEQUENCE, AND
RP VARIANT ASP-42.
RC TISSUE=Bone marrow;
RX PubMed=8248172; DOI=10.1073/pnas.90.22.10793;
RA Chaudhuri A., Polyakova J., Zbrzezna V., Williams K., Gulati S., Pogo A.;
RT "Cloning of glycoprotein D cDNA, which encodes the major subunit of the
RT Duffy blood group system and the receptor for the Plasmodium vivax malaria
RT parasite.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10793-10797(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-42.
RC TISSUE=Blood;
RX PubMed=7663520; DOI=10.1038/ng0695-224;
RA Tournamille C., Colin Y., Cartron J.-P., Le van Kim C.;
RT "Disruption of a GATA motif in the Duffy gene promoter abolishes erythroid
RT gene expression in Duffy-negative individuals.";
RL Nat. Genet. 10:224-228(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=7833467;
RA Iwamoto S., Omi T., Kajii E., Ikemoto S.;
RT "Genomic organization of the glycoprotein D gene: Duffy blood group Fya/Fyb
RT alloantigen system is associated with a polymorphism at the 44-amino acid
RT residue.";
RL Blood 85:622-626(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANTS ASP-42; CYS-89
RP AND THR-100.
RC TISSUE=Blood;
RX PubMed=9731074;
RA Tournamille C., Le Van Kim C., Gane P., Le Pennec P.Y., Roubinet F.,
RA Babinet J., Cartron J.-P., Colin Y.;
RT "Arg89Cys substitution results in very low membrane expression of the Duffy
RT antigen/receptor for chemokines in Fy(x) individuals.";
RL Blood 92:2147-2156(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ASP-42; CYS-89 AND
RP THR-100.
RX PubMed=9886340; DOI=10.1046/j.1365-2141.1998.01083.x;
RA Olsson M.L., Smythe J.S., Hansson C., Poole J., Mallinson G., Jones J.,
RA Avent N.D., Daniels G.;
RT "The Fy(x) phenotype is associated with a missense mutation in the Fy(b)
RT allele predicting Arg89Cys in the Duffy glycoprotein.";
RL Br. J. Haematol. 103:1184-1191(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-326.
RC TISSUE=Peripheral blood;
RA Doescher A.;
RT "New polymorphisms in DARC.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PHE-326.
RC TISSUE=Lung;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117 (ISOFORMS 1 AND 2).
RX PubMed=10570183; DOI=10.1073/pnas.96.24.13973;
RA Zimmerman P.A., Woolley I., Masinde G.L., Miller S.M., McNamara D.T.,
RA Hazlett F., Mgone C.S., Alpers M.P., Genton B., Boatin B.A., Kazura J.W.;
RT "Emergence of FY*A(null) in a Plasmodium vivax-endemic region of Papua New
RT Guinea.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13973-13977(1999).
RN [10]
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-16.
RX PubMed=12956774; DOI=10.1046/j.1365-2141.2003.04533.x;
RA Tournamille C., Filipe A., Wasniowska K., Gane P., Lisowska E.,
RA Cartron J.-P., Colin Y., Le Van Kim C.;
RT "Structure-function analysis of the extracellular domains of the Duffy
RT antigen/receptor for chemokines: characterization of antibody and chemokine
RT binding sites.";
RL Br. J. Haematol. 122:1014-1023(2003).
RN [11]
RP POLYMORPHISM, AND INVOLVEMENT IN RESISTANCE TO MALARIA.
RX PubMed=17389925; DOI=10.1371/journal.pone.0000336;
RA Kasehagen L.J., Mueller I., Kiniboro B., Bockarie M.J., Reeder J.C.,
RA Kazura J.W., Kastens W., McNamara D.T., King C.H., Whalen C.C.,
RA Zimmerman P.A.;
RT "Reduced Plasmodium vivax erythrocyte infection in PNG Duffy-negative
RT heterozygotes.";
RL PLoS ONE 2:E336-E336(2007).
RN [12]
RP REVIEW.
RX PubMed=20373092; DOI=10.1007/82_2010_19;
RA Bonecchi R., Savino B., Borroni E.M., Mantovani A., Locati M.;
RT "Chemokine decoy receptors: structure-function and biological properties.";
RL Curr. Top. Microbiol. Immunol. 341:15-36(2010).
RN [13]
RP REVIEW.
RX PubMed=22912641; DOI=10.3389/fimmu.2012.00266;
RA Novitzky-Basso I., Rot A.;
RT "Duffy antigen receptor for chemokines and its involvement in patterning
RT and control of inflammatory chemokines.";
RL Front. Immunol. 3:266-266(2012).
RN [14]
RP REVIEW.
RX PubMed=22698181; DOI=10.1016/j.imlet.2012.04.004;
RA Graham G.J., Locati M., Mantovani A., Rot A., Thelen M.;
RT "The biochemistry and biology of the atypical chemokine receptors.";
RL Immunol. Lett. 145:30-38(2012).
RN [15]
RP REVIEW.
RX PubMed=23356288; DOI=10.1042/bst20120246;
RA Cancellieri C., Vacchini A., Locati M., Bonecchi R., Borroni E.M.;
RT "Atypical chemokine receptors: from silence to sound.";
RL Biochem. Soc. Trans. 41:231-236(2013).
RN [16]
RP VARIANT ASP-42.
RC TISSUE=Peripheral blood;
RX PubMed=7705836; DOI=10.1007/bf00208965;
RA Tournamille C., Le van Kim C., Gane P., Cartron J.-P., Colin Y.;
RT "Molecular basis and PCR-DNA typing of the Fya/fyb blood group
RT polymorphism.";
RL Hum. Genet. 95:407-410(1995).
RN [17]
RP VARIANT CYS-89.
RX PubMed=9746760;
RA Parasol N., Reid M., Rios M., Castilho L., Harari I., Kosower N.S.;
RT "A novel mutation in the coding sequence of the FY*B allele of the Duffy
RT chemokine receptor gene is associated with an altered erythrocyte
RT phenotype.";
RL Blood 92:2237-2243(1998).
RN [18]
RP INVOLVEMENT IN WBCQ1.
RX PubMed=18179887; DOI=10.1016/j.ajhg.2007.09.003;
RA Nalls M.A., Wilson J.G., Patterson N.J., Tandon A., Zmuda J.M.,
RA Huntsman S., Garcia M., Hu D., Li R., Beamer B.A., Patel K.V.,
RA Akylbekova E.L., Files J.C., Hardy C.L., Buxbaum S.G., Taylor H.A.,
RA Reich D., Harris T.B., Ziv E.;
RT "Admixture mapping of white cell count: genetic locus responsible for lower
RT white blood cell count in the Health ABC and Jackson Heart Studies.";
RL Am. J. Hum. Genet. 82:81-87(2008).
RN [19]
RP ERRATUM OF PUBMED:18179887.
RA Nalls M.A., Wilson J.G., Patterson N.J., Tandon A., Zmuda J.M.,
RA Huntsman S., Garcia M., Hu D., Li R., Beamer B.A., Patel K.V.,
RA Akylbekova E.L., Files J.C., Hardy C.L., Buxbaum S.G., Taylor H.A.,
RA Reich D., Harris T.B., Ziv E.;
RL Am. J. Hum. Genet. 82:532-532(2008).
CC -!- FUNCTION: Atypical chemokine receptor that controls chemokine levels
CC and localization via high-affinity chemokine binding that is uncoupled
CC from classic ligand-driven signal transduction cascades, resulting
CC instead in chemokine sequestration, degradation, or transcytosis. Also
CC known as interceptor (internalizing receptor) or chemokine-scavenging
CC receptor or chemokine decoy receptor. Has a promiscuous chemokine-
CC binding profile, interacting with inflammatory chemokines of both the
CC CXC and the CC subfamilies but not with homeostatic chemokines. Acts as
CC a receptor for chemokines including CCL2, CCL5, CCL7, CCL11, CCL13,
CC CCL14, CCL17, CXCL5, CXCL6, IL8/CXCL8, CXCL11, GRO, RANTES, MCP-1, TARC
CC and also for the malaria parasites P.vivax and P.knowlesi. May regulate
CC chemokine bioavailability and, consequently, leukocyte recruitment
CC through two distinct mechanisms: when expressed in endothelial cells,
CC it sustains the abluminal to luminal transcytosis of tissue-derived
CC chemokines and their subsequent presentation to circulating leukocytes;
CC when expressed in erythrocytes, serves as blood reservoir of cognate
CC chemokines but also as a chemokine sink, buffering potential surges in
CC plasma chemokine levels.
CC -!- INTERACTION:
CC Q16570-1; P22290: PVDR; Xeno; NbExp=3; IntAct=EBI-15935975, EBI-15935953;
CC Q16570-2; P51681: CCR5; NbExp=3; IntAct=EBI-21403047, EBI-489374;
CC -!- SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Membrane;
CC Multi-pass membrane protein. Note=Predominantly localizes to endocytic
CC vesicles, and upon stimulation by the ligand is internalized via
CC caveolae. Once internalized, the ligand dissociates from the receptor,
CC and is targeted to degradation while the receptor is recycled back to
CC the cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q16570-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q16570-2; Sequence=VSP_001323;
CC -!- TISSUE SPECIFICITY: Found in adult kidney, adult spleen, bone marrow
CC and fetal liver. In particular, it is expressed along postcapillary
CC venules throughout the body, except in the adult liver. Erythroid cells
CC and postcapillary venule endothelium are the principle tissues
CC expressing duffy. Fy(-A-B) individuals do not express duffy in the bone
CC marrow, however they do, in postcapillary venule endothelium.
CC -!- POLYMORPHISM: DARC is responsible for the Duffy blood group system (FY)
CC [MIM:110700]. The molecular basis of the Fy(A)=Fy1/Fy(B)=Fy2 blood
CC group antigens is a single variation in position 42; Gly-42 corresponds
CC to Fy(A) and Asp-42 to Fy(B). Individuals that do not produce the Duffy
CC antigen (FY(A-B-)) are more resistant to infection by the malarial
CC parasite Plasmodium vivax. This allele is found predominantly in
CC population of African origin [MIM:611162].
CC -!- POLYMORPHISM: Genetic variations in DARC define the white blood cell
CC count quantitative trait locus 1 (WBCQ1) [MIM:611862]. Peripheral white
CC blood cell count (WBC) is a common clinical measurement, used to
CC determine evidence of acute inflammation or infection. Peripheral WBC
CC is the sum of several cell types including neutrophils and lymphocytes,
CC which are the most common types of WBC, as well as less common cell
CC types such as eosinophils, basophils, and monocytes. Elevated WBC has
CC been associated with risk of coronary heart disease, cancer, and all-
CC cause mortality. White blood cell levels have widespread clinical
CC applications including assessment of patients undergoing chemotherapy
CC and evaluation of infection.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Atypical chemokine receptor subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=duffy";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Duffy antigen entry;
CC URL="https://en.wikipedia.org/wiki/Duffy_antigen";
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DR EMBL; U01839; AAC50055.1; -; mRNA.
DR EMBL; X85785; CAA59770.1; -; Genomic_DNA.
DR EMBL; S76830; AAB33239.1; -; Genomic_DNA.
DR EMBL; AF055992; AAC72301.1; -; Genomic_DNA.
DR EMBL; AF030521; AAD20435.1; -; mRNA.
DR EMBL; AM887935; CAP12644.1; -; Genomic_DNA.
DR EMBL; AL035403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017817; AAH17817.1; -; mRNA.
DR EMBL; AF100634; AAF02415.1; -; Genomic_DNA.
DR EMBL; AF100634; AAF02416.1; -; Genomic_DNA.
DR CCDS; CCDS1183.1; -. [Q16570-1]
DR CCDS; CCDS44252.1; -. [Q16570-2]
DR PIR; I52608; I52608.
DR RefSeq; NP_001116423.1; NM_001122951.2. [Q16570-2]
DR RefSeq; NP_002027.2; NM_002036.3. [Q16570-1]
DR PDB; 4NUU; X-ray; 1.95 A; C=16-43.
DR PDB; 4NUV; X-ray; 2.60 A; C/D=14-43.
DR PDB; 7P93; X-ray; 1.55 A; B/M=34-46.
DR PDBsum; 4NUU; -.
DR PDBsum; 4NUV; -.
DR PDBsum; 7P93; -.
DR AlphaFoldDB; Q16570; -.
DR SMR; Q16570; -.
DR BioGRID; 108808; 3.
DR DIP; DIP-3783N; -.
DR IntAct; Q16570; 3.
DR MINT; Q16570; -.
DR STRING; 9606.ENSP00000357103; -.
DR ChEMBL; CHEMBL2321626; -.
DR TCDB; 9.A.14.13.34; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q16570; 2 sites.
DR iPTMnet; Q16570; -.
DR PhosphoSitePlus; Q16570; -.
DR BioMuta; ACKR1; -.
DR DMDM; 67476970; -.
DR jPOST; Q16570; -.
DR MassIVE; Q16570; -.
DR PaxDb; Q16570; -.
DR PeptideAtlas; Q16570; -.
DR PRIDE; Q16570; -.
DR ProteomicsDB; 60923; -. [Q16570-1]
DR ProteomicsDB; 60924; -. [Q16570-2]
DR ABCD; Q16570; 1 sequenced antibody.
DR Antibodypedia; 2945; 537 antibodies from 41 providers.
DR DNASU; 2532; -.
DR Ensembl; ENST00000368121.6; ENSP00000357103.2; ENSG00000213088.12. [Q16570-2]
DR Ensembl; ENST00000368122.4; ENSP00000357104.1; ENSG00000213088.12. [Q16570-1]
DR Ensembl; ENST00000537147.5; ENSP00000441985.1; ENSG00000213088.12. [Q16570-1]
DR GeneID; 2532; -.
DR KEGG; hsa:2532; -.
DR MANE-Select; ENST00000368122.4; ENSP00000357104.1; NM_002036.4; NP_002027.2.
DR CTD; 2532; -.
DR DisGeNET; 2532; -.
DR GeneCards; ACKR1; -.
DR HGNC; HGNC:4035; ACKR1.
DR HPA; ENSG00000213088; Tissue enhanced (adipose tissue, breast).
DR MalaCards; ACKR1; -.
DR MIM; 110700; phenotype.
DR MIM; 611162; phenotype.
DR MIM; 611862; phenotype.
DR MIM; 613665; gene.
DR neXtProt; NX_Q16570; -.
DR OpenTargets; ENSG00000213088; -.
DR PharmGKB; PA28451; -.
DR VEuPathDB; HostDB:ENSG00000213088; -.
DR eggNOG; ENOG502SNW7; Eukaryota.
DR GeneTree; ENSGT00390000006372; -.
DR HOGENOM; CLU_813693_0_0_1; -.
DR InParanoid; Q16570; -.
DR OMA; FHWQLCP; -.
DR PhylomeDB; Q16570; -.
DR TreeFam; TF105419; -.
DR PathwayCommons; Q16570; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR SignaLink; Q16570; -.
DR BioGRID-ORCS; 2532; 11 hits in 1059 CRISPR screens.
DR ChiTaRS; ACKR1; human.
DR GeneWiki; Duffy_antigen_system; -.
DR GenomeRNAi; 2532; -.
DR Pharos; Q16570; Tbio.
DR PRO; PR:Q16570; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q16570; protein.
DR Bgee; ENSG00000213088; Expressed in vena cava and 168 other tissues.
DR ExpressionAtlas; Q16570; baseline and differential.
DR Genevisible; Q16570; HS.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0019957; F:C-C chemokine binding; IPI:BHF-UCL.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0006952; P:defense response; NAS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0032642; P:regulation of chemokine production; IBA:GO_Central.
DR InterPro; IPR005384; Duffy_chemokine_rcpt.
DR PANTHER; PTHR14181; PTHR14181; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood group antigen;
KW Direct protein sequencing; Disulfide bond; Endosome;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..336
FT /note="Atypical chemokine receptor 1"
FT /id="PRO_0000152585"
FT TOPO_DOM 1..63
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12956774"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..276
FT /evidence="ECO:0000269|PubMed:12956774"
FT DISULFID 129..195
FT /evidence="ECO:0000269|PubMed:12956774"
FT VAR_SEQ 1..7
FT /note="MGNCLHR -> MASSGYVLQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8248172,
FT ECO:0000303|PubMed:9886340"
FT /id="VSP_001323"
FT VARIANT 42
FT /note="G -> D (antigen Fy(b); dbSNP:rs12075)"
FT /evidence="ECO:0000269|PubMed:7663520,
FT ECO:0000269|PubMed:7705836, ECO:0000269|PubMed:8248172,
FT ECO:0000269|PubMed:9731074, ECO:0000269|PubMed:9886340"
FT /id="VAR_003480"
FT VARIANT 89
FT /note="R -> C (antigen Fy(x); dbSNP:rs34599082)"
FT /evidence="ECO:0000269|PubMed:9731074,
FT ECO:0000269|PubMed:9746760, ECO:0000269|PubMed:9886340"
FT /id="VAR_015068"
FT VARIANT 100
FT /note="A -> T (in dbSNP:rs13962)"
FT /evidence="ECO:0000269|PubMed:9731074,
FT ECO:0000269|PubMed:9886340"
FT /id="VAR_015069"
FT VARIANT 203
FT /note="L -> Q (in dbSNP:rs3027020)"
FT /id="VAR_044116"
FT VARIANT 326
FT /note="S -> F (in dbSNP:rs17851570)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6"
FT /id="VAR_044117"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:4NUU"
SQ SEQUENCE 336 AA; 35553 MW; C3F2A3E71D972E2D CRC64;
MGNCLHRAEL SPSTENSSQL DFEDVWNSSY GVNDSFPDGD YGANLEAAAP CHSCNLLDDS
ALPFFILTSV LGILASSTVL FMLFRPLFRW QLCPGWPVLA QLAVGSALFS IVVPVLAPGL
GSTRSSALCS LGYCVWYGSA FAQALLLGCH ASLGHRLGAG QVPGLTLGLT VGIWGVAALL
TLPVTLASGA SGGLCTLIYS TELKALQATH TVACLAIFVL LPLGLFGAKG LKKALGMGPG
PWMNILWAWF IFWWPHGVVL GLDFLVRSKL LLLSTCLAQQ ALDLLLNLAE ALAILHCVAT
PLLLALFCHQ ATRTLLPSLP LPEGWSSHLD TLGSKS
