ID RHCE_HUMAN Reviewed; 417 AA. AC P18577; A7DW68; B7UDF3; B7UDF4; B7UDF5; B7UDF6; B7UDF7; B7UDF8; B7UDF9; AC B7UDG0; B7UDG1; B7UDG2; B7UDG3; Q02163; Q02164; Q02165; Q16160; Q2MJW0; AC Q2VC86; Q3LTM6; Q6AZX5; Q6J2U3; Q7RU06; Q8IZT2; Q8IZT3; Q8IZT4; Q8IZT5; AC Q9UD13; Q9UD14; Q9UD15; Q9UD16; Q9UD73; Q9UD74; Q9UEC2; Q9UEC3; Q9UPN0; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 3. DT 27-MAR-2024, entry version 194. DE RecName: Full=Blood group Rh(CE) polypeptide {ECO:0000305}; DE AltName: Full=Rh polypeptide 1; DE Short=RhPI; DE AltName: Full=Rh30A; DE AltName: Full=RhIXB; DE AltName: Full=Rhesus C/E antigens; DE AltName: CD_antigen=CD240CE; GN Name=RHCE {ECO:0000312|HGNC:HGNC:10008}; Synonyms=RHC, RHE; 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 RHI), AND VARIANTS TRP-16 AND PRO-226. RC TISSUE=Bone marrow; RX PubMed=2123099; DOI=10.1042/bj2710821; RA Avent N.D., Ridgwell K., Tanner M.J.A., Anstee D.J.; RT "cDNA cloning of a 30 kDa erythrocyte membrane protein associated with Rh RT (Rhesus)-blood-group-antigen expression."; RL Biochem. J. 271:821-825(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RHI), PARTIAL PROTEIN SEQUENCE, AND RP VARIANTS TRP-16 AND PRO-226. RC TISSUE=Bone marrow; RX PubMed=1696722; DOI=10.1073/pnas.87.16.6243; RA Cherif-Zahar B., Bloy C., le van Kim C., Blanchard D., Bailly P., RA Hermand P., Salmon C., Cartron J.-P., Colin Y.; RT "Molecular cloning and protein structure of a human blood group Rh RT polypeptide."; RL Proc. Natl. Acad. Sci. U.S.A. 87:6243-6247(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RHIV; RHVI AND RHVIII), AND VARIANT RP TRP-16. 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RHI), AND VARIANTS TRP-16 AND PRO-226. 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 RHI), VARIANT E/RH3 ANTIGEN PRO-226, RP AND POLYMORPHISM. RX PubMed=11380456; DOI=10.1046/j.1365-2141.2001.02803.x; RA Westhoff C.M., Silberstein L.E., Wylie D.E., Skavdahl M., Reid M.E.; RT "16Cys encoded by the RHce gene is associated with altered expression of RT the e antigen and is frequent in the R0 haplotype."; RL Br. J. Haematol. 113:666-671(2001). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RHI), AND VARIANTS TRP-16; ILE-60; RP SER-68; SER-103; VAL-127; ASP-128; THR-154; PRO-226; GLU-233 AND VAL-238. RX PubMed=11724987; DOI=10.1046/j.1537-2995.2001.41111408.x; RA Kashiwase K., Ishikawa Y., Hyodo H., Watanabe Y., Ogawa A., Tsuneyama H., RA Toyoda C., Uchikawa M., Akaza T., Omine M., Juji T.; RT "E variants found in Japanese and c antigenicity alteration without RT substitution in the second extracellular loop."; RL Transfusion 41:1408-1412(2001). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RHI), AND VARIANTS TRP-16; VAL-238; RP VAL-245; GLY-263 AND LYS-267. RX PubMed=12393640; DOI=10.1182/blood-2002-01-0229; RA Noizat-Pirenne F., Lee K., Le Pennec P.-Y., Simon P., Kazup P., Bachir D., RA Rouzaud A.M., Roussel M., Juszczak G., Menanteau C., Rouger P., Kotb R., RA Cartron J.-P., Ansart-Pirenne H.; RT "Rare RHCE phenotypes in black individuals of Afro-Caribbean origin: RT identification and transfusion safety."; RL Blood 100:4223-4231(2002). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RHI), AND VARIANTS ILE-60; SER-68 AND RP SER-103. RA Yan L., Xu X., Zhu F.; RT "A new RhCe allele in Chinese Han population."; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RHI), AND VARIANTS TRP-16; PRO-226; RP GLU-233 AND VAL-245. RA Westhoff C.M., Vege S.; RT "Molecular basis for Crawford antigen expression."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RHI), AND VARIANTS TRP-16; ILE-60; RP SER-68; SER-103 AND PRO-226. RA Vege S., Westhoff C.M.; RT "RHCE gene, allele CE, antigen CE."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RHI). RA Westhoff C.M., Vege S.; RT "RHCE gene, allele RHce, ce antigen."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-16; ILE-60; SER-68; RP SER-103; PRO-226 AND GLU-398. RA Wei Q., Flegel W.A.; RT "RHD allele and RH haplotype distribution in Tibetans."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-16; ILE-60; SER-68; RP SER-103; PRO-226 AND LYS-267. RA Bugert P., Scharberg E.A., Geisen C., von Zabern I., Flegel W.A.; RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases. RN [14] 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 [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM RHI), AND VARIANTS ILE-60; RP SER-68 AND SER-103. RC TISSUE=Brain; 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 [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. RX PubMed=8188244; DOI=10.1006/geno.1994.1014; RA Cherif-Zahar B., le van Kim C., Rouillac C., Raynal V., Cartron J.-P., RA Colin Y.; RT "Organization of the gene (RHCE) encoding the human blood group RhCcEe RT antigens and characterization of the promoter region."; RL Genomics 19:68-74(1994). RN [17] 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 [18] 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 [19] RP NUCLEOTIDE SEQUENCE [MRNA] OF 141-417 (ISOFORMS 1C; 1D; 1H; 2E; 4G; 7A; 8A; RP 8E; 8H; RHIV AND RHVI), AND ALTERNATIVE SPLICING. RC TISSUE=Blood; RX PubMed=7789951; DOI=10.1007/bf00209483; RA Kajii E., Umenishi F., Omi T., Ikemoto S.; RT "Intricate combinatorial patterns of exon splicing generate multiple Rh- RT related isoforms in human erythroid cells."; RL Hum. Genet. 95:657-665(1995). RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] OF 201-417 (ISOFORMS 4G AND RHPI-ALPHA), AND RP TISSUE SPECIFICITY. RC TISSUE=Erythroblast; RX PubMed=8117271; DOI=10.1006/bbrc.1994.1161; RA Umenishi F., Kajii E., Ikemoto S.; RT "Identification of two Rh mRNA isoforms expressed in immature RT erythroblasts."; RL Biochem. Biophys. Res. Commun. 198:1135-1142(1994). RN [21] RP PROTEIN SEQUENCE OF 402-409. 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 [22] RP INVOLVEMENT IN RHNA. RX PubMed=9657769; RA Huang C.H., Chen Y., Reid M.E., Seidl C.; RT "Rhnull disease: the amorph type results from a novel double mutation in RT RhCe gene on D-negative background."; RL Blood 92:664-671(1998). RN [23] RP IDENTIFICATION. RX PubMed=11902138; DOI=10.1182/blood-2001-12-0153; RA Wagner F.F., Flegel W.A.; RT "RHCE represents the ancestral RH position, while RHD is the duplicated RT gene."; RL Blood 99:2272-2273(2002). RN [24] RP INVOLVEMENT IN RHNA. RX PubMed=25413218; DOI=10.1111/trf.12937; RA Silvy M., Beley S., Peyrard T., Ouchari M., Abdelkefi S., Jemni Yacoub S., RA Chiaroni J., Bailly P.; RT "Short duplication within the RHCE gene associated with an in cis deleted RT RHD causing a Rhnull amorph phenotype in an immunized pregnant woman with RT anti-Rh29."; RL Transfusion 55:1407-1410(2015). RN [25] {ECO:0007744|PDB:7UZQ, ECO:0007744|PDB:7V0K, ECO:0007744|PDB:7V0S, ECO:0007744|PDB:8CRT, ECO:0007744|PDB:8CS9, ECO:0007744|PDB:8CSL, ECO:0007744|PDB:8CSX, ECO:0007744|PDB:8CTE} RP STRUCTURE BY ELECTRON MICROSCOPY (2.17 ANGSTROMS), FUNCTION, SUBUNIT, RP ANKYRIN-1 COMPLEX IDENTIFICATION, AND INTERACTION WITH RHAG AND ANK1. RX PubMed=35835865; DOI=10.1038/s41594-022-00792-w; RA Vallese F., Kim K., Yen L.Y., Johnston J.D., Noble A.J., Cali T., RA Clarke O.B.; RT "Architecture of the human erythrocyte ankyrin-1 complex."; RL Nat. Struct. Mol. Biol. 29:706-718(2022). RN [26] RP VARIANTS TRP-16; ILE-60; SER-68 AND SER-103, AND POLYMORPHISM. RX PubMed=8220426; DOI=10.1038/ng0993-62; RA Mouro I., Colin Y., Cherif-Zahar B., Cartron J.-P., le van Kim C.; RT "Molecular genetic basis of the human Rhesus blood group system."; RL Nat. Genet. 5:62-65(1993). CC -!- FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex CC involved in the stability and shape of the erythrocyte membrane CC (PubMed:35835865). Mediates the primary membrane attachment site for CC ANK1 when associated with RHAG (PubMed:35835865). May participate in CC the ammonium and carbon dioxide transport through the heterotrimer form CC (Probable). {ECO:0000269|PubMed:35835865, ECO:0000305}. CC -!- SUBUNIT: Heterotrimer; a RHCE monomer interacts with a RHAG homodimer CC (PubMed:35835865). Component of the ankyrin-1 complex in the CC erythrocyte, composed of ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB CC and AQP1 (PubMed:35835865). Interacts (via the N- and C-terminal) with CC ANK1 (via ANk 1-5 repeats); mediates the primary membrane attachment CC site for ANK1 (PubMed:35835865). {ECO:0000269|PubMed:35835865}. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=14; CC Name=RHI; CC IsoId=P18577-1; Sequence=Displayed; CC Name=RHIV; Synonyms=1e; CC IsoId=P18577-2; Sequence=VSP_005703, VSP_005704; CC Name=RHVI; Synonyms=7c; CC IsoId=P18577-3; Sequence=VSP_005702, VSP_005705; CC Name=RHVIII; CC IsoId=P18577-4; Sequence=VSP_005701; CC Name=1c; CC IsoId=P18577-5; Sequence=VSP_005705; CC Name=1d; CC IsoId=P18577-6; Sequence=VSP_037514; CC Name=1h; CC IsoId=P18577-7; Sequence=VSP_037513; CC Name=2e; CC IsoId=P18577-8; Sequence=VSP_037510, VSP_037512; CC Name=4g; Synonyms=RhPI-Beta; CC IsoId=P18577-9; Sequence=VSP_037509; CC Name=7a; CC IsoId=P18577-10; Sequence=VSP_005702; CC Name=8a; CC IsoId=P18577-11; Sequence=VSP_037506, VSP_037511; CC Name=8e; CC IsoId=P18577-12; Sequence=VSP_037507, VSP_037508; CC Name=8h; CC IsoId=P18577-13; Sequence=VSP_037505; CC Name=RhPI-Alpha; CC IsoId=P18577-14; Sequence=VSP_038405, VSP_038406; CC -!- TISSUE SPECIFICITY: Restricted to tissues or cell lines expressing CC erythroid characters. Isoform 4g and isoform RhPI-Alpha are expressed CC in immature erythroblasts but not in mature erythroblasts. CC {ECO:0000269|PubMed:8117271}. CC -!- POLYMORPHISM: RhCE and RhD are responsible for the RH blood group CC system. The molecular basis of the E=Rh3/e=Rh5 blood group antigens is CC a single variation in position 226; Pro-226 corresponds to Rh3 and Ala- CC 226 to Rh5. Variant p.Trp16Cys is associated with altered expression of CC E antigen. The molecular basis of the C=Rh2/c=Rh4 blood group antigens CC are variations in position 16, 60, 68 and 103; p.Cys16Trp, p.Ile60Leu, CC p.Ser68Asn and p.Ser103Pro are found in antigen Rh4. CC {ECO:0000269|PubMed:11380456, ECO:0000269|PubMed:8220426}. CC -!- DISEASE: Rh-null, amorph type (RHNA) [MIM:617970]: An autosomal CC recessive condition characterized by red blood cells that lack all Rh CC antigens, have increased osmotic fragility, diminished lifespan, and CC show changes in morphology resulting in stomatocytosis. Rh-null CC individuals have mild to moderate hemolytic anemia. They are at risk of CC having adverse reactions in response to transfusion or pregnancy, CC because they may produce antibodies against several of the Rh antigens. CC {ECO:0000269|PubMed:25413218, ECO:0000269|PubMed:9657769}. Note=The CC disease is caused by variants affecting the gene represented in this CC 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; X54534; CAA38401.1; -; mRNA. DR EMBL; M34015; AAA36567.1; -; mRNA. DR EMBL; X63095; CAA44809.1; -; mRNA. DR EMBL; X63096; CAA44810.1; -; mRNA. DR EMBL; X63098; CAA44812.1; -; mRNA. DR EMBL; S57967; AAB26080.1; -; mRNA. DR EMBL; DQ266400; ABB69097.1; -; mRNA. DR EMBL; AB018644; BAA33927.1; -; mRNA. DR EMBL; AB018645; BAA33928.1; -; mRNA. DR EMBL; AB030388; BAA82627.1; -; mRNA. DR EMBL; AB049753; BAB16597.1; -; mRNA. DR EMBL; AF510065; AAN75121.1; -; mRNA. DR EMBL; AF510066; AAN75122.1; -; mRNA. DR EMBL; AF510067; AAN75123.1; -; mRNA. DR EMBL; AF510068; AAN75124.1; -; mRNA. DR EMBL; AY603478; AAT35811.1; -; mRNA. DR EMBL; DQ178642; ABA25912.1; -; mRNA. DR EMBL; DQ266353; ABB97471.1; -; mRNA. DR EMBL; DQ322275; ABC55358.1; -; mRNA. DR EMBL; AM398146; CAL44958.1; -; Genomic_DNA. DR EMBL; FJ486155; ACK75562.1; -; Genomic_DNA. DR EMBL; FJ486156; ACK75563.1; -; Genomic_DNA. DR EMBL; FJ486157; ACK75564.1; -; Genomic_DNA. DR EMBL; FJ486158; ACK75565.1; -; Genomic_DNA. DR EMBL; FJ486159; ACK75566.1; -; Genomic_DNA. DR EMBL; FJ486160; ACK75567.1; -; Genomic_DNA. DR EMBL; FJ486161; ACK75568.1; -; Genomic_DNA. DR EMBL; FJ486162; ACK75569.1; -; Genomic_DNA. DR EMBL; FJ486163; ACK75570.1; -; Genomic_DNA. DR EMBL; FJ486164; ACK75571.1; -; Genomic_DNA. DR EMBL; FJ486165; ACK75572.1; -; Genomic_DNA. DR EMBL; AL031284; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL928711; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC075081; AAH75081.1; -; mRNA. DR EMBL; BC139905; AAI39906.1; -; mRNA. DR EMBL; S70456; AAD14061.1; -; Genomic_DNA. DR EMBL; BN000065; CAD29850.1; -; Genomic_DNA. DR CCDS; CCDS30634.1; -. [P18577-4] DR CCDS; CCDS30635.1; -. [P18577-1] DR CCDS; CCDS30636.1; -. [P18577-3] DR CCDS; CCDS30637.1; -. [P18577-2] DR CCDS; CCDS81283.1; -. [P18577-5] DR PIR; A30405; A30405. DR PIR; I54193; I54193. DR PIR; PC2032; PC2032. DR PIR; PC2033; PC2033. DR PIR; S78478; S78478. DR PIR; S78479; S78479. DR PIR; S78480; S78480. DR RefSeq; NP_065231.3; NM_020485.4. [P18577-1] DR RefSeq; NP_619523.3; NM_138617.3. DR PDB; 7UZQ; EM; 2.17 A; K=1-417. DR PDB; 7V0K; EM; 2.40 A; K=1-417. DR PDB; 7V0S; EM; 2.50 A; K=1-417. DR PDB; 8CRT; EM; 3.00 A; K=1-417. DR PDB; 8CS9; EM; 2.74 A; K=1-417. DR PDB; 8CSL; EM; 25.00 A; K=1-417. DR PDB; 8CSX; EM; 2.40 A; K=1-417. DR PDB; 8CTE; EM; 2.90 A; K=1-417. DR PDBsum; 7UZQ; -. DR PDBsum; 7V0K; -. DR PDBsum; 7V0S; -. DR PDBsum; 8CRT; -. DR PDBsum; 8CS9; -. DR PDBsum; 8CSL; -. DR PDBsum; 8CSX; -. DR PDBsum; 8CTE; -. DR AlphaFoldDB; P18577; -. DR EMDB; EMD-26916; -. DR EMDB; EMD-26943; -. DR EMDB; EMD-26949; -. DR EMDB; EMD-26958; -. DR EMDB; EMD-26960; -. DR EMDB; EMD-26965; -. DR EMDB; EMD-26974; -. DR EMDB; EMD-26988; -. DR SMR; P18577; -. DR STRING; 9606.ENSP00000294413; -. DR TCDB; 1.A.11.4.3; the ammonium transporter channel (amt) family. DR iPTMnet; P18577; -. DR PhosphoSitePlus; P18577; -. DR BioMuta; RHCE; -. DR DMDM; 132558; -. DR jPOST; P18577; -. DR MassIVE; P18577; -. DR PaxDb; 9606-ENSP00000294413; -. DR PeptideAtlas; P18577; -. DR ProteomicsDB; 53578; -. [P18577-1] DR ProteomicsDB; 53579; -. [P18577-10] DR ProteomicsDB; 53580; -. [P18577-11] DR ProteomicsDB; 53583; -. [P18577-14] DR ProteomicsDB; 53584; -. [P18577-2] DR ProteomicsDB; 53586; -. [P18577-4] DR ProteomicsDB; 53587; -. [P18577-5] DR ProteomicsDB; 53588; -. [P18577-6] DR ProteomicsDB; 53589; -. [P18577-7] DR ProteomicsDB; 53590; -. [P18577-8] DR ProteomicsDB; 53591; -. [P18577-9] DR ABCD; P18577; 5 sequenced antibodies. DR Antibodypedia; 15860; 179 antibodies from 25 providers. DR DNASU; 6006; -. DR Ensembl; ENST00000294413.13; ENSP00000294413.6; ENSG00000188672.19. [P18577-1] DR Ensembl; ENST00000340849.8; ENSP00000345084.4; ENSG00000188672.19. [P18577-3] DR Ensembl; ENST00000346452.8; ENSP00000344485.4; ENSG00000188672.19. [P18577-4] DR Ensembl; ENST00000349438.8; ENSP00000334570.5; ENSG00000188672.19. [P18577-2] DR Ensembl; ENST00000413854.5; ENSP00000415417.2; ENSG00000188672.19. [P18577-5] DR GeneID; 6006; -. DR KEGG; hsa:6006; -. DR MANE-Select; ENST00000294413.13; ENSP00000294413.6; NM_020485.8; NP_065231.4. DR UCSC; uc001bkf.4; human. [P18577-1] DR AGR; HGNC:10008; -. DR CTD; 6006; -. DR DisGeNET; 6006; -. DR GeneCards; RHCE; -. DR HGNC; HGNC:10008; RHCE. DR HPA; ENSG00000188672; Tissue enriched (bone). DR MalaCards; RHCE; -. DR MIM; 111700; gene. DR MIM; 617970; phenotype. DR neXtProt; NX_P18577; -. DR OpenTargets; ENSG00000188672; -. DR Orphanet; 71275; Rh deficiency syndrome. DR PharmGKB; PA34386; -. DR VEuPathDB; HostDB:ENSG00000188672; -. DR eggNOG; KOG3796; Eukaryota. DR GeneTree; ENSGT00950000182844; -. DR HOGENOM; CLU_021386_1_0_1; -. DR InParanoid; P18577; -. DR OrthoDB; 5483564at2759; -. DR PhylomeDB; P18577; -. DR TreeFam; TF314450; -. DR PathwayCommons; P18577; -. DR Reactome; R-HSA-9037628; Rhesus blood group biosynthesis. DR SIGNOR; P18577; -. DR BioGRID-ORCS; 6006; 19 hits in 1148 CRISPR screens. DR ChiTaRS; RHCE; human. DR GeneWiki; RHCE_(gene); -. DR GenomeRNAi; 6006; -. DR Pharos; P18577; Tbio. DR PRO; PR:P18577; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P18577; Protein. DR Bgee; ENSG00000188672; Expressed in trabecular bone tissue and 107 other cell types or tissues. DR ExpressionAtlas; P18577; baseline and differential. DR GO; GO:0170014; C:ankyrin-1 complex; IDA:UniProtKB. 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; P18577; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Blood group antigen; KW Direct protein sequencing; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:3135863, FT ECO:0000269|PubMed:3146980" FT CHAIN 2..417 FT /note="Blood group Rh(CE) polypeptide" FT /id="PRO_0000168189" 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 125..145 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 172..192 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 265..285 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 287..307 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 331..351 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 358..378 FT /note="Helical" FT /evidence="ECO:0000255" FT VAR_SEQ 163..409 FT /note="Missing (in isoform 8h)" FT /evidence="ECO:0000303|PubMed:7789951" FT /id="VSP_037505" FT VAR_SEQ 163..313 FT /note="Missing (in isoform RHVIII)" FT /evidence="ECO:0000303|PubMed:1379850" FT /id="VSP_005701" FT VAR_SEQ 163..220 FT /note="Missing (in isoform 8a)" FT /evidence="ECO:0000303|PubMed:7789951" FT /id="VSP_037506" FT VAR_SEQ 163..203 FT /note="TDYHMNLRHFYVFAAYFGLTVAWCLPKPLPKGTEDNDQRAT -> DWLPGPP FT QHWGTQLGHRDSSHVWSPDRFAPKSQNMESTSCG (in isoform 8e)" FT /evidence="ECO:0000303|PubMed:7789951" FT /id="VSP_037507" FT VAR_SEQ 164..268 FT /note="Missing (in isoform RHVI and isoform 7a)" FT /evidence="ECO:0000303|PubMed:1379850, FT ECO:0000303|PubMed:7789951" FT /id="VSP_005702" FT VAR_SEQ 204..417 FT /note="Missing (in isoform 8e)" FT /evidence="ECO:0000303|PubMed:7789951" FT /id="VSP_037508" FT VAR_SEQ 212..384 FT /note="Missing (in isoform 4g)" FT /evidence="ECO:0000303|PubMed:7789951, FT ECO:0000303|PubMed:8117271" FT /id="VSP_037509" FT VAR_SEQ 227..242 FT /note="LLRSPIQRKNAMFNTY -> DRFAPKSQNMESTSCG (in isoform FT RhPI-Alpha)" FT /evidence="ECO:0000303|PubMed:8117271" FT /id="VSP_038405" FT VAR_SEQ 243..417 FT /note="Missing (in isoform RhPI-Alpha)" FT /evidence="ECO:0000303|PubMed:8117271" FT /id="VSP_038406" FT VAR_SEQ 268..308 FT /note="TYVHSAVLAGGVAVGTSCHLIPSPWLAMVLGLVAGLISIGG -> DWLPGPP FT QHWGTQLGHRDSSHVWSPDRFAPKSQNMESTSCG (in isoform 2e)" FT /evidence="ECO:0000303|PubMed:7789951" FT /id="VSP_037510" FT VAR_SEQ 301..313 FT /note="Missing (in isoform 8a)" FT /evidence="ECO:0000303|PubMed:7789951" FT /id="VSP_037511" FT VAR_SEQ 309..417 FT /note="Missing (in isoform 2e)" FT /evidence="ECO:0000303|PubMed:7789951" FT /id="VSP_037512" FT VAR_SEQ 314..409 FT /note="Missing (in isoform 1h)" FT /evidence="ECO:0000303|PubMed:7789951" FT /id="VSP_037513" FT VAR_SEQ 314..354 FT /note="VCCNRVLGIHHISVMHSIFSLLGLLGEITYIVLLVLHTVWN -> DWLPGPP FT QHWGTQLGHRDSSHVWSPDRFAPKSQNMESTSCG (in isoform RHIV)" FT /evidence="ECO:0000303|PubMed:1379850, FT ECO:0000303|PubMed:7789951" FT /id="VSP_005703" FT VAR_SEQ 355..417 FT /note="Missing (in isoform RHIV)" FT /evidence="ECO:0000303|PubMed:1379850, FT ECO:0000303|PubMed:7789951" FT /id="VSP_005704" FT VAR_SEQ 358..417 FT /note="MIGFQVLLSIGELSLAIVIALTSGLLTGLLLNLKIWKAPHVAKYFDDQVFWK FT FPHLAVGF -> IFLIWLLDFKQKHPRKTRPVQKQDNFLSLLPAVREKRS (in FT isoform 1d)" FT /evidence="ECO:0000303|PubMed:7789951" FT /id="VSP_037514" FT VAR_SEQ 359..417 FT /note="IGFQVLLSIGELSLAIVIALTSGLLTGLLLNLKIWKAPHVAKYFDDQVFWKF FT PHLAVGF -> FAPKSQNMESTSCG (in isoform RHVI and isoform 1c)" FT /evidence="ECO:0000303|PubMed:1379850, FT ECO:0000303|PubMed:7789951" FT /id="VSP_005705" FT VARIANT 16 FT /note="C -> W (found in antigen c/Rh4)" FT /evidence="ECO:0000269|PubMed:11380456, FT ECO:0000269|PubMed:11724987, ECO:0000269|PubMed:12393640, FT ECO:0000269|PubMed:1379850, ECO:0000269|PubMed:1696722, FT ECO:0000269|PubMed:2123099, ECO:0000269|PubMed:7916743, FT ECO:0000269|PubMed:8220426, ECO:0000269|Ref.10, FT ECO:0000269|Ref.12, ECO:0000269|Ref.13, ECO:0000269|Ref.9" FT /id="VAR_006911" FT VARIANT 36 FT /note="A -> T (in C(X)/Rh9 antigen; dbSNP:rs145034271)" FT /id="VAR_006912" FT VARIANT 41 FT /note="Q -> R (found in antigen C(W)/Rh8; FT dbSNP:rs138268848)" FT /id="VAR_006913" FT VARIANT 60 FT /note="L -> I (found in antigen C/Rh2; dbSNP:rs181860403)" FT /evidence="ECO:0000269|PubMed:11724987, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8220426, FT ECO:0000269|Ref.10, ECO:0000269|Ref.12, ECO:0000269|Ref.13, FT ECO:0000269|Ref.8" FT /id="VAR_006914" FT VARIANT 68 FT /note="N -> S (found in antigen C/Rh2; dbSNP:rs1053344)" FT /evidence="ECO:0000269|PubMed:11724987, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8220426, FT ECO:0000269|Ref.10, ECO:0000269|Ref.12, ECO:0000269|Ref.13, FT ECO:0000269|Ref.8" FT /id="VAR_006915" FT VARIANT 103 FT /note="P -> S (found in antigen C/Rh2; dbSNP:rs676785)" FT /evidence="ECO:0000269|PubMed:11724987, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8220426, FT ECO:0000269|Ref.10, ECO:0000269|Ref.12, ECO:0000269|Ref.13, FT ECO:0000269|Ref.8" FT /id="VAR_006916" FT VARIANT 127 FT /note="A -> V (in dbSNP:rs1053346)" FT /evidence="ECO:0000269|PubMed:11724987" FT /id="VAR_055260" FT VARIANT 128 FT /note="G -> D (in dbSNP:rs1053347)" FT /evidence="ECO:0000269|PubMed:11724987" FT /id="VAR_055261" FT VARIANT 154 FT /note="R -> T (found in antigen RhEKH)" FT /evidence="ECO:0000269|PubMed:11724987" FT /id="VAR_013301" FT VARIANT 182 FT /note="T -> S (in dbSNP:rs1053350)" FT /id="VAR_055262" FT VARIANT 198 FT /note="N -> K (in dbSNP:rs1053354)" FT /id="VAR_055263" FT VARIANT 226 FT /note="A -> P (found in antigen E/Rh3; dbSNP:rs609320)" FT /evidence="ECO:0000269|PubMed:11380456, FT ECO:0000269|PubMed:11724987, ECO:0000269|PubMed:12393640, FT ECO:0000269|PubMed:1379850, ECO:0000269|PubMed:1696722, FT ECO:0000269|PubMed:2123099, ECO:0000269|PubMed:7916743, FT ECO:0000269|PubMed:8220426, ECO:0000269|Ref.10, FT ECO:0000269|Ref.12, ECO:0000269|Ref.13, ECO:0000269|Ref.9" FT /id="VAR_006917" FT VARIANT 233 FT /note="Q -> E (found in antigen RhEFM; dbSNP:rs142246017)" FT /evidence="ECO:0000269|PubMed:11724987, ECO:0000269|Ref.9" FT /id="VAR_013302" FT VARIANT 238 FT /note="M -> V (found in antigen RhEFM; dbSNP:rs144163296)" FT /evidence="ECO:0000269|PubMed:11724987, FT ECO:0000269|PubMed:12393640" FT /id="VAR_013303" FT VARIANT 245 FT /note="L -> V (in VS antigen; dbSNP:rs1053361)" FT /evidence="ECO:0000269|PubMed:12393640, ECO:0000269|Ref.9" FT /id="VAR_006918" FT VARIANT 263 FT /note="R -> G (in dbSNP:rs1132763)" FT /evidence="ECO:0000269|PubMed:12393640" FT /id="VAR_057987" FT VARIANT 267 FT /note="M -> K (in dbSNP:rs1132764)" FT /evidence="ECO:0000269|PubMed:12393640, ECO:0000269|Ref.13" FT /id="VAR_057988" FT VARIANT 323 FT /note="H -> P (in dbSNP:rs1053366)" FT /id="VAR_055264" FT VARIANT 325 FT /note="I -> S (in dbSNP:rs1053367)" FT /id="VAR_055265" FT VARIANT 329 FT /note="H -> D (in dbSNP:rs1053370)" FT /id="VAR_055266" FT VARIANT 329 FT /note="H -> R (in dbSNP:rs1053371)" FT /id="VAR_055267" FT VARIANT 330 FT /note="S -> Y (in dbSNP:rs1053372)" FT /id="VAR_055268" FT VARIANT 331 FT /note="I -> N (in dbSNP:rs1053373)" FT /id="VAR_055269" FT VARIANT 398 FT /note="V -> E (in dbSNP:rs630612)" FT /evidence="ECO:0000269|Ref.12" FT /id="VAR_057989" FT CONFLICT 10 FT /note="R -> W (in Ref. 13; ACK75562)" FT /evidence="ECO:0000305" FT CONFLICT 12 FT /note="C -> L (in Ref. 18; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 53 FT /note="D -> G (in Ref. 3; CAA44812)" FT /evidence="ECO:0000305" FT CONFLICT 61 FT /note="G -> C (in Ref. 3; CAA44812)" FT /evidence="ECO:0000305" FT CONFLICT 114 FT /note="R -> W (in Ref. 7; AAN75123)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="L -> P (in Ref. 13; ACK75563/ACK75565)" FT /evidence="ECO:0000305" FT CONFLICT 121 FT /note="M -> L (in Ref. 6; BAB16597/BAA82627)" FT /evidence="ECO:0000305" FT CONFLICT 122 FT /note="S -> P (in Ref. 13; ACK75564)" FT /evidence="ECO:0000305" FT CONFLICT 125 FT /note="I -> N (in Ref. 13; ACK75565)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="T -> N (in Ref. 6; BAB16597/BAA82627)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="M -> V (in Ref. 8; AAT35811)" FT /evidence="ECO:0000305" FT CONFLICT 166 FT /note="H -> L (in Ref. 13; ACK75566)" FT /evidence="ECO:0000305" FT CONFLICT 169 FT /note="L -> Q (in Ref. 13; ACK75567)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="R -> T (in Ref. 13; ACK75568)" FT /evidence="ECO:0000305" FT CONFLICT 217 FT /note="W -> R (in Ref. 13; ACK75569)" FT /evidence="ECO:0000305" FT CONFLICT 241 FT /note="T -> I (in Ref. 13; ACK75570)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="V -> M (in Ref. 7; AAN75124)" FT /evidence="ECO:0000305" FT CONFLICT 273 FT /note="A -> V (in Ref. 7; AAN75122)" FT /evidence="ECO:0000305" FT CONFLICT 303 FT /note="L -> Q (in Ref. 13; ACK75572)" FT /evidence="ECO:0000305" FT CONFLICT 378 FT /note="L -> V (in Ref. 7; AAN75122)" FT /evidence="ECO:0000305" FT CONFLICT 408..409 FT /note="WK -> DI (in Ref. 21; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 12..31 FT /evidence="ECO:0007829|PDB:7UZQ" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:8CSX" FT HELIX 44..59 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 61..65 FT /evidence="ECO:0007829|PDB:7UZQ" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:7UZQ" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 73..98 FT /evidence="ECO:0007829|PDB:7UZQ" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:8CSX" FT HELIX 110..127 FT /evidence="ECO:0007829|PDB:7UZQ" FT TURN 128..132 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 136..161 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 167..171 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 172..186 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 203..219 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 220..222 FT /evidence="ECO:0007829|PDB:7UZQ" FT STRAND 224..227 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 231..256 FT /evidence="ECO:0007829|PDB:7UZQ" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:7UZQ" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 267..273 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 276..280 FT /evidence="ECO:0007829|PDB:7UZQ" FT TURN 281..287 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 291..311 FT /evidence="ECO:0007829|PDB:7UZQ" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 327..347 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 361..388 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 398..400 FT /evidence="ECO:0007829|PDB:7UZQ" FT HELIX 404..406 FT /evidence="ECO:0007829|PDB:7UZQ" SQ SEQUENCE 417 AA; 45451 MW; 0EEB9D726DB28E6C CRC64; MSSKYPRSVR RCLPLCALTL EAALILLFYF FTHYDASLED QKGLVASYQV GQDLTVMAAL GLGFLTSNFR RHSWSSVAFN LFMLALGVQW AILLDGFLSQ FPPGKVVITL FSIRLATMSA MSVLISAGAV LGKVNLAQLV VMVLVEVTAL GTLRMVISNI FNTDYHMNLR HFYVFAAYFG LTVAWCLPKP LPKGTEDNDQ RATIPSLSAM LGALFLWMFW PSVNSALLRS PIQRKNAMFN TYYALAVSVV TAISGSSLAH PQRKISMTYV HSAVLAGGVA VGTSCHLIPS PWLAMVLGLV AGLISIGGAK CLPVCCNRVL GIHHISVMHS IFSLLGLLGE ITYIVLLVLH TVWNGNGMIG FQVLLSIGEL SLAIVIALTS GLLTGLLLNL KIWKAPHVAK YFDDQVFWKF PHLAVGF //