RHD_HUMAN
ID RHD_HUMAN Reviewed; 417 AA.
AC Q02161; Q02162; Q07618; Q16147; Q16235; Q16355; Q5VSK0; Q5XLS9; Q5XLT1;
AC Q5XLT2; Q9NPK0; Q9UQ20; Q9UQ21; Q9UQ22; Q9UQ23;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Blood group Rh(D) polypeptide;
DE AltName: Full=RHXIII;
DE AltName: Full=Rh polypeptide 2;
DE Short=RhPII;
DE AltName: Full=Rhesus D antigen;
DE AltName: CD_antigen=CD240D;
GN Name=RHD;
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 VARIANT ILE-218.
RC TISSUE=Bone marrow;
RX PubMed=1438298; DOI=10.1073/pnas.89.22.10925;
RA le van Kim C., Mouro I., Cherif-Zahar B., Raynal V., Cherrier C.,
RA Cartron J.-P., Colin Y.;
RT "Molecular cloning and primary structure of the human blood group RhD
RT polypeptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10925-10929(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=1379850;
RA le van Kim C., Cherif-Zahar B., Raynal V., Mouro I., Lopez M.,
RA Cartron J.-P., Colin Y.;
RT "Multiple Rh messenger RNA isoforms are produced by alternative splicing.";
RL Blood 80:1074-1078(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8329718;
RA Arce M.A., Thompson E.S., Wagner S., Coyne K.E., Ferdman B.A., Lublin D.M.;
RT "Molecular cloning of RhD cDNA derived from a gene present in RhD-positive,
RT but not RhD-negative individuals.";
RL Blood 82:651-655(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-182.
RX PubMed=7916743; DOI=10.1007/bf00222717;
RA Kajii E., Umenishi F., Iwamoto S., Ikemoto S.;
RT "Isolation of a new cDNA clone encoding an Rh polypeptide associated with
RT the Rh blood group system.";
RL Hum. Genet. 91:157-162(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8180407;
RA Westhoff C.M., Wylie D.E.;
RT "Identification of a new RhD-specific mRNA from K562 cells.";
RL Blood 83:3098-3100(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-16.
RX PubMed=7606008;
RA Huang C.-H., Reid M.E., Chen Y.;
RT "Identification of a partial internal deletion in the RH locus causing the
RT human erythrocyte D-phenotype.";
RL Blood 86:784-790(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=8080999;
RA Suyama K., Lunn R., Haller S., Goldstein J.;
RT "Rh(D) antigen expression and isolation of a new Rh(D) cDNA isoform in
RT human erythroleukemic K562 cells.";
RL Blood 84:1975-1981(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6), AND ALTERNATIVE SPLICING.
RX PubMed=16510313; DOI=10.1016/j.transci.2005.10.001;
RA Shao C.P., Xiong W., Zhou Y.Y.;
RT "Multiple isoforms excluding normal RhD mRNA detected in Rh blood group Del
RT phenotype with RHD 1227A allele.";
RL Transfus. Apher. Sci. 34:145-152(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-223; GLN-233; MET-238 AND
RP LEU-245.
RA Hyodo H., Ishikawa Y., Kashiwase K., Ogawa A., Watanabe Y., Tsuneyama H.,
RA Toyoda C., Uchikawa M., Akaza T., Fujii T.;
RT "Polymorphisms of RhDVa in Japanese.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
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 [11]
RP PROTEIN SEQUENCE OF 2-33.
RX PubMed=3146980; DOI=10.1042/bj2561043;
RA Avent N.D., Ridgwell K., Mawby W.J., Tanner M.J.A., Anstee D.J., Kumpel B.;
RT "Protein-sequence studies on Rh-related polypeptides suggest the presence
RT of at least two groups of proteins which associate in the human red-cell
RT membrane.";
RL Biochem. J. 256:1043-1046(1988).
RN [12]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=3131772; DOI=10.1073/pnas.85.11.4042;
RA Saboori A.M., Smith B.L., Agre P.;
RT "Polymorphism in the Mr 32,000 Rh protein purified from Rh(D)-positive and
RT -negative erythrocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4042-4045(1988).
RN [13]
RP PROTEIN SEQUENCE OF 2-17.
RX PubMed=3135863;
RA Bloy C., Blanchard D., Dahr W., Beyreuther K., Salmon C., Cartron J.-P.;
RT "Determination of the N-terminal sequence of human red cell Rh(D)
RT polypeptide and demonstration that the Rh(D), (c), and (E) antigens are
RT carried by distinct polypeptide chains.";
RL Blood 72:661-666(1988).
RN [14]
RP PROTEIN SEQUENCE OF 401-407.
RX PubMed=1898705;
RA Suyama K., Goldstein J., Aebersold R., Kent S.;
RT "Regarding the size of Rh proteins.";
RL Blood 77:411-411(1991).
RN [15]
RP SUBCELLULAR LOCATION, AND PALMITOYLATION.
RX PubMed=3142870; DOI=10.1016/s0021-9258(19)81344-3;
RA de Vetten M.P., Agre P.;
RT "The Rh polypeptide is a major fatty acid-acylated erythrocyte membrane
RT protein.";
RL J. Biol. Chem. 263:18193-18196(1988).
RN [16]
RP INVOLVEMENT IN RH BLOOD GROUP SYSTEM.
RX PubMed=1824267;
RA Colin Y., Cherif-Zahar B., Le Van Kim C., Raynal V., Van Huffel V.,
RA Cartron J.P.;
RT "Genetic basis of the RhD-positive and RhD-negative blood group
RT polymorphism as determined by Southern analysis.";
RL Blood 78:2747-2752(1991).
RN [17]
RP SUBCELLULAR LOCATION, AND PALMITOYLATION.
RX PubMed=1544931; DOI=10.1016/s0021-9258(18)42803-7;
RA Hartel-Schenk S., Agre P.;
RT "Mammalian red cell membrane Rh polypeptides are selectively palmitoylated
RT subunits of a macromolecular complex.";
RL J. Biol. Chem. 267:5569-5574(1992).
RN [18]
RP INVOLVEMENT IN RH BLOOD GROUP SYSTEM, AND VARIANTS CYS-3; GLN-10; ASP-149;
RP THR-182; ASN-198; ARG-201; ARG-220; VAL-223; GLY-270; PRO-276; GLU-277;
RP ASP-282; ILE-283; PRO-294; ILE-295; ARG-307; GLU-339; ALA-385 AND ARG-393.
RX PubMed=9864185;
RA Wagner F.F., Gassner C., Mueller T.H., Schoenitzer D., Schunter F.,
RA Flegel W.A.;
RT "Molecular basis of weak D phenotypes.";
RL Blood 93:385-393(1999).
RN [19]
RP INVOLVEMENT IN RH BLOOD GROUP SYSTEM.
RX PubMed=10845894;
RA Wagner F.F., Flegel W.A.;
RT "RHD gene deletion occurred in the Rhesus box.";
RL Blood 95:3662-3668(2000).
RN [20]
RP INVOLVEMENT IN HDFNRH.
RX PubMed=10805260; DOI=10.1054/blre.1999.0123;
RA Urbaniak S.J., Greiss M.A.;
RT "RhD haemolytic disease of the fetus and the newborn.";
RL Blood Rev. 14:44-61(2000).
RN [21]
RP VARIANT TAR ANTIGEN PRO-110.
RX PubMed=7741145; DOI=10.1002/ajh.2830490115;
RA Rouillac C., le van Kim C., Beolet M., Cartron J.-P., Colin Y.;
RT "Leu110Pro substitution in the RhD polypeptide is responsible for the DVII
RT category blood group phenotype.";
RL Am. J. Hematol. 49:87-88(1995).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-103.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be part of an oligomeric complex which is likely to have
CC a transport or channel function in the erythrocyte membrane.
CC -!- INTERACTION:
CC Q02161-2; Q13520: AQP6; NbExp=3; IntAct=EBI-17249212, EBI-13059134;
CC Q02161-2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-17249212, EBI-6942903;
CC Q02161-2; P15941-11: MUC1; NbExp=3; IntAct=EBI-17249212, EBI-17263240;
CC Q02161-2; Q9NY72: SCN3B; NbExp=3; IntAct=EBI-17249212, EBI-17247926;
CC Q02161-2; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-17249212, EBI-17280858;
CC Q02161-2; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-17249212, EBI-8638294;
CC Q02161-2; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-17249212, EBI-10982110;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1544931,
CC ECO:0000269|PubMed:3142870}; Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Long;
CC IsoId=Q02161-1; Sequence=Displayed;
CC Name=2; Synonyms=Short 1;
CC IsoId=Q02161-2; Sequence=VSP_005706;
CC Name=3; Synonyms=Short 2;
CC IsoId=Q02161-3; Sequence=VSP_005707, VSP_005708;
CC Name=4;
CC IsoId=Q02161-4; Sequence=VSP_047797;
CC Name=5;
CC IsoId=Q02161-5; Sequence=VSP_047796;
CC Name=6;
CC IsoId=Q02161-6; Sequence=VSP_047795, VSP_047798;
CC -!- TISSUE SPECIFICITY: Restricted to tissues or cell lines expressing
CC erythroid characters.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:1544931,
CC ECO:0000269|PubMed:3142870}.
CC -!- POLYMORPHISM: RHD and RHCE are responsible for the Rh blood group
CC system. The molecular basis of the Tar=Rh40 blood group antigen is a
CC variant in position 110. Homozygous deletion of the RHD gene results in
CC Rh-negative (dd) individuals (PubMed:1824267, PubMed:10845894). Some
CC polymorhisms lead to weak RHD expression. This phenotype called weak D,
CC formerly known as D(u), is observed in about 0.2% to 1% of Caucasians
CC (PubMed:9864185). Moderately decreased RHD expression results in a
CC phenotype called DHMi (PubMed:9864185). {ECO:0000269|PubMed:10845894,
CC ECO:0000269|PubMed:1824267, ECO:0000269|PubMed:9864185}.
CC -!- DISEASE: Hemolytic disease of fetus and newborn, RH-induced (HDFNRH)
CC [MIM:619462]: A disease that occurs in pregnancies in which mothers who
CC lack the D antigen (RhD) of the Rh blood group have been exposed to the
CC RhD-positive red cells of the fetus. The resulting maternal
CC autoantibodies cross the placenta and destroy fetal red cells.
CC {ECO:0000269|PubMed:10805260}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh
CC 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=rh";
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DR EMBL; X63097; CAA44811.1; -; mRNA.
DR EMBL; X63094; CAA44808.1; -; mRNA.
DR EMBL; L08429; AAA02679.1; -; mRNA.
DR EMBL; S57971; AAB26081.1; -; mRNA.
DR EMBL; S70174; AAB30756.1; -; mRNA.
DR EMBL; S78509; AAB34852.1; -; mRNA.
DR EMBL; S73913; AAB31911.1; -; mRNA.
DR EMBL; AY751492; AAU93636.1; -; mRNA.
DR EMBL; AY751493; AAU93637.1; -; mRNA.
DR EMBL; AY751495; AAU93639.1; -; mRNA.
DR EMBL; AB018966; BAA81899.1; -; mRNA.
DR EMBL; AB018967; BAA81900.1; -; mRNA.
DR EMBL; AB018968; BAA81901.1; -; mRNA.
DR EMBL; AB018969; BAA82159.1; -; mRNA.
DR EMBL; AL928711; CAH72602.1; -; Genomic_DNA.
DR CCDS; CCDS262.1; -. [Q02161-1]
DR CCDS; CCDS53285.1; -. [Q02161-2]
DR CCDS; CCDS60028.1; -. [Q02161-4]
DR CCDS; CCDS60030.1; -. [Q02161-5]
DR CCDS; CCDS60031.1; -. [Q02161-6]
DR PIR; A46368; A46368.
DR PIR; I52615; I52615.
DR RefSeq; NP_001121163.1; NM_001127691.2. [Q02161-2]
DR RefSeq; NP_001269797.1; NM_001282868.1. [Q02161-6]
DR RefSeq; NP_001269798.1; NM_001282869.1. [Q02161-5]
DR RefSeq; NP_001269800.1; NM_001282871.1. [Q02161-4]
DR RefSeq; NP_057208.2; NM_016124.4. [Q02161-1]
DR AlphaFoldDB; Q02161; -.
DR SMR; Q02161; -.
DR BioGRID; 111939; 8.
DR IntAct; Q02161; 7.
DR ChEMBL; CHEMBL3712996; -.
DR TCDB; 1.A.11.4.3; the ammonium transporter channel (amt) family.
DR iPTMnet; Q02161; -.
DR PhosphoSitePlus; Q02161; -.
DR BioMuta; RHD; -.
DR DMDM; 296452980; -.
DR jPOST; Q02161; -.
DR MassIVE; Q02161; -.
DR PaxDb; Q02161; -.
DR PeptideAtlas; Q02161; -.
DR PRIDE; Q02161; -.
DR ProteomicsDB; 58055; -. [Q02161-1]
DR ProteomicsDB; 65840; -.
DR ABCD; Q02161; 105 sequenced antibodies.
DR Antibodypedia; 30382; 237 antibodies from 25 providers.
DR DNASU; 6007; -.
DR Ensembl; ENST00000328664.9; ENSP00000331871.4; ENSG00000187010.21. [Q02161-1]
DR Ensembl; ENST00000342055.9; ENSP00000339577.5; ENSG00000187010.21. [Q02161-4]
DR Ensembl; ENST00000357542.8; ENSP00000350150.4; ENSG00000187010.21. [Q02161-5]
DR Ensembl; ENST00000417538.6; ENSP00000396420.2; ENSG00000187010.21. [Q02161-6]
DR Ensembl; ENST00000454452.6; ENSP00000413849.2; ENSG00000187010.21. [Q02161-2]
DR GeneID; 6007; -.
DR KEGG; hsa:6007; -.
DR MANE-Select; ENST00000328664.9; ENSP00000331871.4; NM_016124.6; NP_057208.3.
DR UCSC; uc001bjz.5; human. [Q02161-1]
DR CTD; 6007; -.
DR DisGeNET; 6007; -.
DR GeneCards; RHD; -.
DR HGNC; HGNC:10009; RHD.
DR HPA; ENSG00000187010; Tissue enriched (bone).
DR MalaCards; RHD; -.
DR MIM; 111680; gene.
DR MIM; 619462; phenotype.
DR neXtProt; NX_Q02161; -.
DR OpenTargets; ENSG00000187010; -.
DR Orphanet; 71275; Rh deficiency syndrome.
DR PharmGKB; PA34387; -.
DR VEuPathDB; HostDB:ENSG00000187010; -.
DR GeneTree; ENSGT00950000182844; -.
DR HOGENOM; CLU_021386_1_0_1; -.
DR InParanoid; Q02161; -.
DR OMA; DQAYWEF; -.
DR PhylomeDB; Q02161; -.
DR TreeFam; TF314450; -.
DR PathwayCommons; Q02161; -.
DR Reactome; R-HSA-9037628; Rhesus blood group biosynthesis.
DR SignaLink; Q02161; -.
DR BioGRID-ORCS; 6007; 10 hits in 1035 CRISPR screens.
DR ChiTaRS; RHD; human.
DR GeneWiki; RHD_(gene); -.
DR GenomeRNAi; 6007; -.
DR Pharos; Q02161; Tbio.
DR PRO; PR:Q02161; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q02161; protein.
DR Bgee; ENSG00000187010; Expressed in buccal mucosa cell and 100 other tissues.
DR ExpressionAtlas; Q02161; baseline and differential.
DR Genevisible; Q02161; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0097272; P:ammonium homeostasis; IBA:GO_Central.
DR GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.10.3430.10; -; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR InterPro; IPR002229; RhesusRHD.
DR Pfam; PF00909; Ammonium_transp; 1.
DR PRINTS; PR00342; RHESUSRHD.
PE 1: Evidence at protein level;
KW Alternative splicing; Blood group antigen; Cell membrane;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3131772,
FT ECO:0000269|PubMed:3135863, ECO:0000269|PubMed:3146980"
FT CHAIN 2..417
FT /note="Blood group Rh(D) polypeptide"
FT /id="PRO_0000168190"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 314..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8180407"
FT /id="VSP_005706"
FT VAR_SEQ 314..378
FT /note="GCCNRVLGIPHSSIMGYNFSLLGLLGEIIYIVLLVLDTVGAGNGMIGFQVLL
FT SIGELSLAIVIAL -> DWLPGPPQHWGTQLGHRDSSHVWSPDSFLIWLLDFKQKHPRK
FT TRPVQKQDNFLSLLPAFVREKRS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16510313"
FT /id="VSP_047795"
FT VAR_SEQ 316
FT /note="C -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8080999"
FT /id="VSP_005707"
FT VAR_SEQ 317..417
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8080999"
FT /id="VSP_005708"
FT VAR_SEQ 358..417
FT /note="MIGFQVLLSIGELSLAIVIALMSGLLTGLLLNLKIWKAPHEAKYFDDQVFWK
FT FPHLAVGF -> IFLIWLLDFKQKHPRKTRPVQKQDNFLSLLPAFVREKRS (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:16510313"
FT /id="VSP_047796"
FT VAR_SEQ 359..417
FT /note="IGFQVLLSIGELSLAIVIALMSGLLTGLLLNLKIWKAPHEAKYFDDQVFWKF
FT PHLAVGF -> SLGWNLAVKMAEAGDEELMRLDVSQRNHGGAAVPTGSWMPSTETTIAP
FT NYRDHISVVSSFGCWILSKSIQEKQGLFKNKTTSSHCCLHLYVRNAHDSKVSNVRAGTG
FT VRENGVESFLCHSLRRISPFIMHCRIQQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16510313"
FT /id="VSP_047797"
FT VAR_SEQ 379..417
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16510313"
FT /id="VSP_047798"
FT VARIANT 3
FT /note="S -> C (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086023"
FT VARIANT 10
FT /note="R -> Q (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086024"
FT VARIANT 16
FT /note="W -> C (in dbSNP:rs772865539)"
FT /evidence="ECO:0000269|PubMed:7606008"
FT /id="VAR_034455"
FT VARIANT 103
FT /note="S -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035615"
FT VARIANT 110
FT /note="L -> P (in Tar antigen; dbSNP:rs121912762)"
FT /evidence="ECO:0000269|PubMed:7741145"
FT /id="VAR_006919"
FT VARIANT 149
FT /note="A -> D (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086025"
FT VARIANT 182
FT /note="S -> T (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:7916743,
FT ECO:0000269|PubMed:9864185"
FT /id="VAR_086026"
FT VARIANT 193
FT /note="E -> K (in dbSNP:rs1053352)"
FT /id="VAR_034456"
FT VARIANT 198
FT /note="K -> N (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086027"
FT VARIANT 201
FT /note="T -> R (may be associated with low RHD expression,
FT resulting in a weak D phenotype; dbSNP:rs1053355)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_034457"
FT VARIANT 218
FT /note="M -> I (in dbSNP:rs141540728)"
FT /evidence="ECO:0000269|PubMed:1438298"
FT /id="VAR_006920"
FT VARIANT 220
FT /note="W -> R (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086028"
FT VARIANT 223
FT /note="F -> V (found in RhDVa(FK) and RhDVa(TT); may be
FT associated with low RHD expression, resulting in a weak D
FT phenotype; dbSNP:rs1053356)"
FT /evidence="ECO:0000269|PubMed:9864185, ECO:0000269|Ref.9"
FT /id="VAR_013304"
FT VARIANT 233
FT /note="E -> Q (found in RhDVa(FK), RhDVa(TO), RhDVa(TT) and
FT RhDYo; dbSNP:rs1053359)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_013305"
FT VARIANT 238
FT /note="V -> M (found in RhDVa(TO) and RhDVa(TT);
FT dbSNP:rs1053360)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_013306"
FT VARIANT 245
FT /note="V -> L (found in RhDVa(TT); dbSNP:rs150073306)"
FT /evidence="ECO:0000269|Ref.9"
FT /id="VAR_013307"
FT VARIANT 263
FT /note="G -> R (in dbSNP:rs3118454)"
FT /id="VAR_047996"
FT VARIANT 270
FT /note="V -> G (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086029"
FT VARIANT 276
FT /note="A -> P (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086030"
FT VARIANT 277
FT /note="G -> E (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086031"
FT VARIANT 282
FT /note="G -> D (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086032"
FT VARIANT 283
FT /note="T -> I (may be associated with moderate decrease in
FT RHD expression, resulting in DHMi phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086033"
FT VARIANT 294
FT /note="A -> P (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086034"
FT VARIANT 295
FT /note="M -> I (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086035"
FT VARIANT 306
FT /note="V -> I (in dbSNP:rs590813)"
FT /id="VAR_047997"
FT VARIANT 307
FT /note="G -> R (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086036"
FT VARIANT 311
FT /note="Y -> C (in dbSNP:rs590787)"
FT /id="VAR_047998"
FT VARIANT 339
FT /note="G -> E (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086037"
FT VARIANT 385
FT /note="G -> A (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086038"
FT VARIANT 393
FT /note="W -> R (may be associated with low RHD expression,
FT resulting in a weak D phenotype)"
FT /evidence="ECO:0000269|PubMed:9864185"
FT /id="VAR_086039"
FT CONFLICT 39
FT /note="E -> G (in Ref. 4; AAB26081)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="S -> P (in Ref. 4; AAB26081)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="V -> A (in Ref. 4; AAB26081)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="V -> M (in Ref. 6; AAB34852)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="G -> V (in Ref. 4; AAB26081 and 7; AAB31911)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="P -> H (in Ref. 4; AAB26081)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="M -> T (in Ref. 1; CAA44811/CAA44808, 3; AAA02679,
FT 4; AAB26081, 6; AAB34852 and 8; BAA81899/BAA81900/BAA81901/
FT BAA82159)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="E -> V (in Ref. 6; AAB34852)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 417 AA; 45211 MW; 38721BFA664AE199 CRC64;
MSSKYPRSVR RCLPLWALTL EAALILLFYF FTHYDASLED QKGLVASYQV GQDLTVMAAI
GLGFLTSSFR RHSWSSVAFN LFMLALGVQW AILLDGFLSQ FPSGKVVITL FSIRLATMSA
LSVLISVDAV LGKVNLAQLV VMVLVEVTAL GNLRMVISNI FNTDYHMNMM HIYVFAAYFG
LSVAWCLPKP LPEGTEDKDQ TATIPSLSAM LGALFLWMFW PSFNSALLRS PIERKNAVFN
TYYAVAVSVV TAISGSSLAH PQGKISKTYV HSAVLAGGVA VGTSCHLIPS PWLAMVLGLV
AGLISVGGAK YLPGCCNRVL GIPHSSIMGY NFSLLGLLGE IIYIVLLVLD TVGAGNGMIG
FQVLLSIGEL SLAIVIALMS GLLTGLLLNL KIWKAPHEAK YFDDQVFWKF PHLAVGF
