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 27-MAR-2024, entry version 195. 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"; 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; 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 PeptideAtlas; Q02161; -. DR ProteomicsDB; 58055; -. [Q02161-1] DR ProteomicsDB; 65840; -. DR ABCD; Q02161; 105 sequenced antibodies. DR Antibodypedia; 30382; 306 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 AGR; HGNC:10009; -. 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; CEATFLP; -. DR OrthoDB; 5483564at2759; -. 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; 12 hits in 1114 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 102 other cell types or tissues. DR ExpressionAtlas; Q02161; baseline and differential. 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; Ammonium transporter AmtB like domains; 1. DR InterPro; IPR029020; Ammonium/urea_transptr. DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom. DR InterPro; IPR002229; RhesusRHD. DR PANTHER; PTHR11730; AMMONIUM TRANSPORTER; 1. DR PANTHER; PTHR11730:SF43; BLOOD GROUP RH(CE) POLYPEPTIDE-RELATED; 1. DR Pfam; PF00909; Ammonium_transp; 1. DR PRINTS; PR00342; RHESUSRHD. DR SUPFAM; SSF111352; Ammonium transporter; 1. DR Genevisible; Q02161; HS. 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; FT BAA81899/BAA81900/BAA81901/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 //