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Q9H310 (RHBG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ammonium transporter Rh type B
Alternative name(s):
Rhesus blood group family type B glycoprotein
Short name=Rh family type B glycoprotein
Short name=Rh type B glycoprotein
Gene names
Name:RHBG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as a specific ammonium transporter. Ref.7 Ref.8

Subunit structure

Interacts (via C-terminus) with ANK2 and ANK3; required for targeting to the basolateral membrane. Ref.9

Subcellular location

Basolateral cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein Ref.1 Ref.9.

Tissue specificity

Specifically expressed in kidney. Also detected in liver and ovary. Ref.1

Developmental stage

Fetally expressed by kidney and to a lower extent in liver. Ref.1

Post-translational modification

N-glycosylated By similarity. Ref.1

Sequence similarities

Belongs to the ammonium transporter (TC 2.A.49) family. Rh subfamily. [View classification]

Sequence caution

The sequence AAG01086.1 differs from that shown. Reason: Frameshift at position 425.

The sequence AAL05978.1 differs from that shown. Reason: Frameshift at position 425.

The sequence AAN34363.1 differs from that shown. Reason: Frameshift at position 425.

The sequence AAN34364.1 differs from that shown. Reason: Frameshift at position 425.

Ontologies

Keywords
   Biological processAmmonia transport
Transport
   Cellular componentCell membrane
Cytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Uncategorized?

Inferred from direct assay. Source: UniProtKB

   Biological_processammonium transmembrane transport

Inferred from direct assay Ref.8PubMed 18032481PubMed 18635543. Source: GOC

ammonium transport

Inferred from direct assay Ref.8PubMed 18032481PubMed 18635543. Source: UniProtKB

transepithelial ammonium transport

Inferred from direct assay PubMed 18032481. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentanchored component of plasma membrane

Inferred from mutant phenotype Ref.9. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay Ref.9PubMed 18635543. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.8. Source: UniProtKB

spectrin-associated cytoskeleton

Inferred from mutant phenotype PubMed 18635543. Source: UniProtKB

   Molecular_functionammonium transmembrane transporter activity

Inferred from direct assay Ref.8PubMed 18032481PubMed 18635543. Source: UniProtKB

ankyrin binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H310-1)

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: Q9H310-2)

Also known as: RhBG-2A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     31-63: AVFVRYNHKTDAALWHRSNHSNADNEFYFRYPS → MNFTFATQKSLTLLPRLECNGAISAHCNLHLPG
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9H310-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.
     175-175: G → GVRVWGGMESGVGGGQGQPLSQERGGGGGVLPLTPPPQ
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9H310-4)

Also known as: RhBG-1A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.
Isoform 5 (identifier: Q9H310-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.
     372-441: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441Ammonium transporter Rh type B
PRO_0000283597

Regions

Topological domain1 – 1313Cytoplasmic Potential
Transmembrane14 – 3421Helical; Potential
Topological domain35 – 6127Extracellular Potential
Transmembrane62 – 8221Helical; Potential
Topological domain83 – 864Cytoplasmic Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 12417Extracellular Potential
Transmembrane125 – 14521Helical; Potential
Topological domain146 – 1494Cytoplasmic Potential
Transmembrane150 – 17021Helical; Potential
Topological domain171 – 1788Extracellular Potential
Transmembrane179 – 20123Helical; Potential
Topological domain202 – 21918Cytoplasmic Potential
Transmembrane220 – 24021Helical; Potential
Topological domain241 – 25111Extracellular Potential
Transmembrane252 – 27221Helical; Potential
Topological domain273 – 28210Cytoplasmic Potential
Transmembrane283 – 30321Helical; Potential
Topological domain3041Extracellular Potential
Transmembrane305 – 32521Helical; Potential
Topological domain326 – 34621Cytoplasmic Potential
Transmembrane347 – 36721Helical; Potential
Topological domain368 – 39326Extracellular Potential
Transmembrane394 – 41421Helical; Potential
Topological domain415 – 44127Cytoplasmic Potential
Region416 – 4249Interaction with ANK3

Amino acid modifications

Glycosylation491N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 6969Missing in isoform 3, isoform 4 and isoform 5.
VSP_024340
Alternative sequence1 – 3030Missing in isoform 2.
VSP_024341
Alternative sequence31 – 6333AVFVR…FRYPS → MNFTFATQKSLTLLPRLECN GAISAHCNLHLPG in isoform 2.
VSP_024342
Alternative sequence1751G → GVRVWGGMESGVGGGQGQPL SQERGGGGGVLPLTPPPQ in isoform 3.
VSP_024343
Alternative sequence372 – 44170Missing in isoform 5.
VSP_037136
Natural variant761G → D. Ref.3 Ref.5
Corresponds to variant rs2245623 [ dbSNP | Ensembl ].
VAR_031497
Natural variant1431V → D. Ref.6
Corresponds to variant rs11586833 [ dbSNP | Ensembl ].
VAR_031498
Natural variant3151G → R. Ref.6
Corresponds to variant rs3748569 [ dbSNP | Ensembl ].
VAR_031499
Natural variant3391C → R.
Corresponds to variant rs3748567 [ dbSNP | Ensembl ].
VAR_053637

Experimental info

Mutagenesis4191F → A: Loss of interaction with ANK3. Intracellular retention; when associated with A-420 and A-421. Ref.9
Mutagenesis4201L → A: Partial loss of interaction with ANK3. Intracellular retention; when associated with A-419 and A-421. Ref.9
Mutagenesis4211D → A: Partial loss of interaction with ANK3. Intracellular retention; when associated with A-419 and A-420. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 21EE1FE592F2E1EE

FASTA44147,231
        10         20         30         40         50         60 
MAGSPSRAAG RRLQLPLLCL FLQGATAVLF AVFVRYNHKT DAALWHRSNH SNADNEFYFR 

        70         80         90        100        110        120 
YPSFQDVHAM VFVGFGFLMV FLQRYGFSSV GFTFLLAAFA LQWSTLVQGF LHSFHGGHIH 

       130        140        150        160        170        180 
VGVESMINAD FCAGAVLISF GAVLGKTGPT QLLLMALLEV VLFGINEFVL LHLLGVRDAG 

       190        200        210        220        230        240 
GSMTIHTFGA YFGLVLSRVL YRPQLEKSKH RQGSVYHSDL FAMIGTIFLW IFWPSFNAAL 

       250        260        270        280        290        300 
TALGAGQHRT ALNTYYSLAA STLGTFALSA LVGEDGRLDM VHIQNAALAG GVVVGTSSEM 

       310        320        330        340        350        360 
MLTPFGALAA GFLAGTVSTL GYKFFTPILE SKFKVQDTCG VHNLHGMPGV LGALLGVLVA 

       370        380        390        400        410        420 
GLATHEAYGD GLESVFPLIA EGQRSATSQA MHQLFGLFVT LMFASVGGGL GGLLLKLPFL 

       430        440 
DSPPRLPALR GPSSLAGAWR A 

« Hide

Isoform 2 (RhBG-2A) [UniParc].

Checksum: B9C06223F4445B97
Show »

FASTA41143,675
Isoform 3 [UniParc].

Checksum: D0FE23FCAC1344ED
Show »

FASTA40942,978
Isoform 4 (RhBG-1A) [UniParc].

Checksum: 47C840C8A19763F5
Show »

FASTA37239,396
Isoform 5 [UniParc].

Checksum: B758ABDDBA1E2E90
Show »

FASTA30232,092

References

« Hide 'large scale' references
[1]"Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals."
Liu Z., Peng J., Mo R., Hui C.-C., Huang C.-H.
J. Biol. Chem. 276:1424-1433(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
Tissue: Liver.
[2]"Characterization of alternatively spliced Rh type B glycoprotein (RhBG) isoforms in human tissues resulting from exonic inclusion of Alu repeat like sequences."
Liu Z., Chen Y., Huang C.-H.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
Tissue: Liver.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), VARIANT ASP-76.
Tissue: Cerebellum and Liver.
[4]"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. expand/collapse author list , 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].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASP-76.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANTS ASP-143 AND ARG-315.
Tissue: Ovary.
[7]"Electroneutral ammonium transport by basolateral rhesus B glycoprotein."
Ludewig U.
J. Physiol. (Lond.) 559:751-759(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells."
Zidi-Yahiaoui N., Mouro-Chanteloup I., D'Ambrosio A.-M., Lopez C., Gane P., Le van Kim C., Cartron J.-P., Colin Y., Ripoche P.
Biochem. J. 391:33-40(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells."
Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R., Bennett V., Cartron J.-P., Le Van Kim C., Colin Y.
J. Biol. Chem. 280:8221-8228(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-419; LEU-420 AND ASP-421, INTERACTION WITH ANK2 AND ANK3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF193807 mRNA. Translation: AAG01086.1. Frameshift.
AF219980 expand/collapse EMBL AC list , AF219977, AF219978, AF219979 Genomic DNA. Translation: AAL05978.1. Frameshift.
AY139092 mRNA. Translation: AAN34363.1. Frameshift.
AY139093 mRNA. Translation: AAN34364.1. Frameshift.
AK054780 mRNA. Translation: BAG51423.1.
AK290840 mRNA. Translation: BAF83529.1.
AL589685, AL139130 Genomic DNA. Translation: CAI14175.1.
AL589685, AL139130 Genomic DNA. Translation: CAI14176.1.
AL589685, AL139130 Genomic DNA. Translation: CAI14177.1.
AL139130, AL589685 Genomic DNA. Translation: CAI12178.1.
AL139130, AL589685 Genomic DNA. Translation: CAI12179.1.
AL139130, AL589685 Genomic DNA. Translation: CAI12180.1.
CH471121 Genomic DNA. Translation: EAW52961.1.
BC065218 mRNA. Translation: AAH65218.1.
RefSeqNP_001243324.1. NM_001256395.1.
NP_001243325.1. NM_001256396.1.
NP_065140.3. NM_020407.4.
UniGeneHs.131835.

3D structure databases

ProteinModelPortalQ9H310.
SMRQ9H310. Positions 12-423.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121390. 1 interaction.
IntActQ9H310. 1 interaction.
STRING9606.ENSP00000255013.

Protein family/group databases

TCDB1.A.11.4.2. the ammonia transporter channel (amt) family.

Polymorphism databases

DMDM209572666.

Proteomic databases

PaxDbQ9H310.
PRIDEQ9H310.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255013; ENSP00000255013; ENSG00000132677. [Q9H310-4]
ENST00000368249; ENSP00000357232; ENSG00000132677. [Q9H310-1]
ENST00000400992; ENSP00000383777; ENSG00000132677. [Q9H310-3]
GeneID57127.
KEGGhsa:57127.
UCSCuc009wrz.4. human. [Q9H310-3]
uc010pho.3. human. [Q9H310-1]
uc031pqo.1. human. [Q9H310-2]

Organism-specific databases

CTD57127.
GeneCardsGC01P156339.
HGNCHGNC:14572. RHBG.
HPAHPA048489.
MIM607079. gene.
neXtProtNX_Q9H310.
PharmGKBPA34385.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276393.
HOVERGENHBG004374.
KOK06580.
PhylomeDBQ9H310.
TreeFamTF314450.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
REACT_20679. Amine compound SLC transporters.

Gene expression databases

ArrayExpressQ9H310.
BgeeQ9H310.
GenevestigatorQ9H310.

Family and domain databases

InterProIPR024041. NH4_transpt_AmtB-like_dom.
IPR002229. RhesusRHD.
[Graphical view]
PfamPF00909. Ammonium_transp. 1 hit.
[Graphical view]
PRINTSPR00342. RHESUSRHD.
SUPFAMSSF111352. SSF111352. 1 hit.
ProtoNetSearch...

Other

GeneWikiRHBG.
GenomeRNAi57127.
NextBio63029.
PROQ9H310.
SOURCESearch...

Entry information

Entry nameRHBG_HUMAN
AccessionPrimary (citable) accession number: Q9H310
Secondary accession number(s): A8K475 expand/collapse secondary AC list , Q5SZW4, Q5SZW6, Q5SZW7, Q6P193, Q6YJI2, Q6YJI3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 14, 2008
Last modified: April 16, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM