Q02161 (RHD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Blood group Rh(D) polypeptide

Alternative name(s):
RHXIII
Rh polypeptide 2
Short name=RhPII
Rhesus D antigen
CD_antigen=CD240D

Gene names

Name:

RHD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	417 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Restricted to tissues or cell lines expressing erythroid characters.
Polymorphism	RHD and RHCE are responsible for the Rh blood group system. The molecular basis of the Tar=Rh40 blood group antigen is a polymorphism in position 110.
Sequence similarities	Belongs to the ammonium transporter (TC 2.A.49) family. Rh subfamily. [View classification]

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Blood group antigen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ammonium transmembrane transport Inferred from electronic annotation. Source: GOC
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	ammonium transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q02161-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q02161-2)

Also known as: Short 1;

The sequence of this isoform differs from the canonical sequence as follows:
     314-409: Missing.

Isoform 3 (identifier: Q02161-3)

Also known as: Short 2;

The sequence of this isoform differs from the canonical sequence as follows:
     316-316: C → S
     317-417: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.10 Ref.11 Ref.12
	Chain	2 – 417	416	Blood group Rh(D) polypeptide		PRO_0000168190
Regions
	Transmembrane	12 – 32	21	Helical; Potential
	Transmembrane	44 – 64	21	Helical; Potential
	Transmembrane	77 – 97	21	Helical; Potential
	Transmembrane	107 – 127	21	Helical; Potential
	Transmembrane	130 – 150	21	Helical; Potential
	Transmembrane	167 – 187	21	Helical; Potential
	Transmembrane	203 – 223	21	Helical; Potential
	Transmembrane	238 – 258	21	Helical; Potential
	Transmembrane	287 – 307	21	Helical; Potential
	Transmembrane	334 – 354	21	Helical; Potential
	Transmembrane	358 – 378	21	Helical; Potential
Natural variations
	Alternative sequence	314 – 409	96	Missing in isoform 2.		VSP_005706
	Alternative sequence	316	1	C → S in isoform 3.		VSP_005707
	Alternative sequence	317 – 417	101	Missing in isoform 3.		VSP_005708
	Natural variant	16	1	W → C. Ref.6 Corresponds to variant rs586178 [ dbSNP | Ensembl ].		VAR_034455
	Natural variant	103	1	S → C in a breast cancer sample; somatic mutation. Ref.15		VAR_035615
	Natural variant	110	1	L → P in Tar antigen. Ref.14		VAR_006919
	Natural variant	193	1	E → K. Corresponds to variant rs17418091 [ dbSNP | Ensembl ].		VAR_034456
	Natural variant	201	1	T → R. Corresponds to variant rs17418098 [ dbSNP | Ensembl ].		VAR_034457
	Natural variant	218	1	M → I. Ref.1		VAR_006920
	Natural variant	223	1	F → V in RhDVa(FK) and RhDVa(TT). Ref.8		VAR_013304
	Natural variant	233	1	E → Q in RhDVa(FK), RhDVa(TO), RhDVa(TT) and RhDYo. Ref.8 Corresponds to variant rs1053359 [ dbSNP | Ensembl ].		VAR_013305
	Natural variant	238	1	V → M in RhDVa(TO) and RhDVa(TT). Ref.8 Corresponds to variant rs1053360 [ dbSNP | Ensembl ].		VAR_013306
	Natural variant	245	1	V → L in RhDVa(TT). Ref.8		VAR_013307
	Natural variant	263	1	G → R. Corresponds to variant rs3118454 [ dbSNP | Ensembl ].		VAR_047996
	Natural variant	306	1	V → I. Corresponds to variant rs590813 [ dbSNP | Ensembl ].		VAR_047997
	Natural variant	311	1	Y → C. Corresponds to variant rs590787 [ dbSNP | Ensembl ].		VAR_047998
Experimental info
	Sequence conflict	39	1	E → G in AAB26081. Ref.4
	Sequence conflict	103	1	S → P in AAB26081. Ref.4
	Sequence conflict	127	1	V → A in AAB26081. Ref.4
	Sequence conflict	174	1	V → M in AAB34852. Ref.6
	Sequence conflict	182	1	S → T in AAB26081. Ref.4
	Sequence conflict	314	1	G → V in AAB26081. Ref.4
	Sequence conflict	314	1	G → V in AAB31911. Ref.7
	Sequence conflict	323	1	P → H in AAB26081. Ref.4
	Sequence conflict	379	1	M → T in CAA44811. Ref.1
	Sequence conflict	379	1	M → T in CAA44808. Ref.1
	Sequence conflict	379	1	M → T in AAA02679. Ref.3
	Sequence conflict	379	1	M → T in AAB26081. Ref.4
	Sequence conflict	379	1	M → T in AAB34852. Ref.6
	Sequence conflict	379	1	M → T in BAA81899. Ref.8
	Sequence conflict	379	1	M → T in BAA81900. Ref.8
	Sequence conflict	379	1	M → T in BAA81901. Ref.8
	Sequence conflict	379	1	M → T in BAA82159. Ref.8
	Sequence conflict	398	1	E → V in AAB34852. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 38721BFA664AE199	FASTA	417	45,211
	10 20 30 40 50 60 MSSKYPRSVR RCLPLWALTL EAALILLFYF FTHYDASLED QKGLVASYQV GQDLTVMAAI 70 80 90 100 110 120 GLGFLTSSFR RHSWSSVAFN LFMLALGVQW AILLDGFLSQ FPSGKVVITL FSIRLATMSA 130 140 150 160 170 180 LSVLISVDAV LGKVNLAQLV VMVLVEVTAL GNLRMVISNI FNTDYHMNMM HIYVFAAYFG 190 200 210 220 230 240 LSVAWCLPKP LPEGTEDKDQ TATIPSLSAM LGALFLWMFW PSFNSALLRS PIERKNAVFN 250 260 270 280 290 300 TYYAVAVSVV TAISGSSLAH PQGKISKTYV HSAVLAGGVA VGTSCHLIPS PWLAMVLGLV 310 320 330 340 350 360 AGLISVGGAK YLPGCCNRVL GIPHSSIMGY NFSLLGLLGE IIYIVLLVLD TVGAGNGMIG 370 380 390 400 410 FQVLLSIGEL SLAIVIALMS GLLTGLLLNL KIWKAPHEAK YFDDQVFWKF PHLAVGF
	Isoform 2 (Short 1) [UniParc]. Checksum: 79E9FB671F8F84E8	FASTA	321	34,837
	10 20 30 40 50 60 MSSKYPRSVR RCLPLWALTL EAALILLFYF FTHYDASLED QKGLVASYQV GQDLTVMAAI 70 80 90 100 110 120 GLGFLTSSFR RHSWSSVAFN LFMLALGVQW AILLDGFLSQ FPSGKVVITL FSIRLATMSA 130 140 150 160 170 180 LSVLISVDAV LGKVNLAQLV VMVLVEVTAL GNLRMVISNI FNTDYHMNMM HIYVFAAYFG 190 200 210 220 230 240 LSVAWCLPKP LPEGTEDKDQ TATIPSLSAM LGALFLWMFW PSFNSALLRS PIERKNAVFN 250 260 270 280 290 300 TYYAVAVSVV TAISGSSLAH PQGKISKTYV HSAVLAGGVA VGTSCHLIPS PWLAMVLGLV 310 320 AGLISVGGAK YLPFPHLAVG F
	Isoform 3 (Short 2) [UniParc]. Checksum: 4BCD39AC4813587F	FASTA	316	34,215
	10 20 30 40 50 60 MSSKYPRSVR RCLPLWALTL EAALILLFYF FTHYDASLED QKGLVASYQV GQDLTVMAAI 70 80 90 100 110 120 GLGFLTSSFR RHSWSSVAFN LFMLALGVQW AILLDGFLSQ FPSGKVVITL FSIRLATMSA 130 140 150 160 170 180 LSVLISVDAV LGKVNLAQLV VMVLVEVTAL GNLRMVISNI FNTDYHMNMM HIYVFAAYFG 190 200 210 220 230 240 LSVAWCLPKP LPEGTEDKDQ TATIPSLSAM LGALFLWMFW PSFNSALLRS PIERKNAVFN 250 260 270 280 290 300 TYYAVAVSVV TAISGSSLAH PQGKISKTYV HSAVLAGGVA VGTSCHLIPS PWLAMVLGLV 310 AGLISVGGAK YLPGCS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and primary structure of the human blood group RhD polypeptide." le van Kim C., Mouro I., Cherif-Zahar B., Raynal V., Cherrier C., Cartron J.-P., Colin Y. Proc. Natl. Acad. Sci. U.S.A. 89:10925-10929(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-218. Tissue: Bone marrow.
[2]	"Multiple Rh messenger RNA isoforms are produced by alternative splicing." le van Kim C., Cherif-Zahar B., Raynal V., Mouro I., Lopez M., Cartron J.-P., Colin Y. Blood 80:1074-1078(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Bone marrow.
[3]	"Molecular cloning of RhD cDNA derived from a gene present in RhD-positive, but not RhD-negative individuals." Arce M.A., Thompson E.S., Wagner S., Coyne K.E., Ferdman B.A., Lublin D.M. Blood 82:651-655(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Isolation of a new cDNA clone encoding an Rh polypeptide associated with the Rh blood group system." Kajii E., Umenishi F., Iwamoto S., Ikemoto S. Hum. Genet. 91:157-162(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Identification of a new RhD-specific mRNA from K562 cells." Westhoff C.M., Wylie D.E. Blood 83:3098-3100(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[6]	"Identification of a partial internal deletion in the RH locus causing the human erythrocyte D-phenotype." Huang C.-H., Reid M.E., Chen Y. Blood 86:784-790(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-16.
[7]	"Rh(D) antigen expression and isolation of a new Rh(D) cDNA isoform in human erythroleukemic K562 cells." Suyama K., Lunn R., Haller S., Goldstein J. Blood 84:1975-1981(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[8]	"Polymorphisms of RhDVa in Japanese." Hyodo H., Ishikawa Y., Kashiwase K., Ogawa A., Watanabe Y., Tsuneyama H., Toyoda C., Uchikawa M., Akaza T., Fujii T. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-223; GLN-233; MET-238 AND LEU-245.
[9]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane." Avent N.D., Ridgwell K., Mawby W.J., Tanner M.J.A., Anstee D.J., Kumpel B. Biochem. J. 256:1043-1046(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-33.
[11]	"Polymorphism in the Mr 32,000 Rh protein purified from Rh(D)-positive and -negative erythrocytes." Saboori A.M., Smith B.L., Agre P. Proc. Natl. Acad. Sci. U.S.A. 85:4042-4045(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21.
[12]	"Determination of the N-terminal sequence of human red cell Rh(D) polypeptide and demonstration that the Rh(D), (c), and (E) antigens are carried by distinct polypeptide chains." Bloy C., Blanchard D., Dahr W., Beyreuther K., Salmon C., Cartron J.-P. Blood 72:661-666(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-17.
[13]	"Regarding the size of Rh proteins." Suyama K., Goldstein J., Aebersold R., Kent S. Blood 77:411-411(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 401-407.
[14]	"Leu110Pro substitution in the RhD polypeptide is responsible for the DVII category blood group phenotype." Rouillac C., le van Kim C., Beolet M., Cartron J.-P., Colin Y. Am. J. Hematol. 49:87-88(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TAR ANTIGEN PRO-110.
[15]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-103.
+	Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	X63097 mRNA. Translation: CAA44811.1. X63094 mRNA. Translation: CAA44808.1. L08429 mRNA. Translation: AAA02679.1. S57971 mRNA. Translation: AAB26081.1. S70174 mRNA. Translation: AAB30756.1. S78509 mRNA. Translation: AAB34852.1. S73913 mRNA. Translation: AAB31911.1. AB018966 mRNA. Translation: BAA81899.1. AB018967 mRNA. Translation: BAA81900.1. AB018968 mRNA. Translation: BAA81901.1. AB018969 mRNA. Translation: BAA82159.1. AL928711 Genomic DNA. Translation: CAH72602.1.
IPI	IPI00478571. IPI00869023. IPI00941406.
PIR	A46368. I52615.
RefSeq	NP_001121163.1. NM_001127691.1. NP_057208.2. NM_016124.3.
UniGene	Hs.449968.
3D structure databases
ProteinModelPortal	Q02161.
SMR	Q02161. Positions 40-308.
ModBase	Search...
Protein family/group databases
TCDB	1.A.11.4.3. ammonia transporter channel (Amt) family.
PTM databases
PhosphoSite	Q02161.
Polymorphism databases
DMDM	296452980.
Proteomic databases
PaxDb	Q02161.
PRIDE	Q02161.
Protocols and materials databases
DNASU	6007.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000328664; ENSP00000331871; ENSG00000187010. ENST00000454452; ENSP00000413849; ENSG00000187010.
GeneID	6007.
KEGG	hsa:6007.
UCSC	uc009vrm.3. human.
Organism-specific databases
CTD	6007.
GeneCards	GC01P025599.
HGNC	HGNC:10009. RHD.
MIM	111680. gene.
neXtProt	NX_Q02161.
Orphanet	71275. Rh deficiency syndrome.
PharmGKB	PA34387.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG314742.
HOVERGEN	HBG004374.
KO	K06579.
OrthoDB	EOG4H464H.
PhylomeDB	Q02161.
Gene expression databases
ArrayExpress	Q02161.
Bgee	Q02161.
Genevestigator	Q02161.
GermOnline	ENSG00000187010. Homo sapiens.
Family and domain databases
InterPro	IPR024041. NH4_transpt_AmtB-like_dom. IPR002229. RhesusRHD. [Graphical view]
Pfam	PF00909. Ammonium_transp. 1 hit. [Graphical view]
PRINTS	PR00342. RHESUSRHD.
SUPFAM	SSF111352. RH_like_transpt. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	6007.
NextBio	23439.
SOURCE	Search...

Entry information

Entry name

RHD_HUMAN

Accession

Primary (citable) accession number: Q02161
Secondary accession number(s): Q02162 , Q07618, Q16147, Q16235, Q16355, Q5VSK0, Q9NPK0, Q9UQ20, Q9UQ21, Q9UQ22, Q9UQ23

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.