Q9UHX3 (EMR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
EGF-like module-containing mucin-like hormone receptor-like 2

Alternative name(s):
EGF-like module receptor 2
CD_antigen=CD312

Gene names

Name:

EMR2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	823 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	Receptor probably involved in cell attachment.
Subunit structure	Forms a heterodimer, consisting of a large extracellular region non-covalently linked to a seven-transmembrane moiety. Interacts with chondroitin sulfate. Ref.5 Ref.7
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Expression is restricted to myeloid cells. Highest expression was found in peripheral blood leukocytes, followed by spleen and lymph nodes, with intermediate to low levels in thymus, bone marrow, fetal liver, placenta, and lung, and no expression in heart, brain, skeletal muscle, kidney, or pancreas. Expression is also detected in monocyte/macrophage and Jurkat cell lines but not in other cell lines tested. Ref.1 Ref.6
Domain	The GPS domain is necessary, but not sufficient for receptor cleavage, which require the entire extracellular stalk. Binding to chondroitin sulfate is mediated by the fourth EGF domain.
Post-translational modification	Autoproteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane beta subunit. Ref.4 Ref.7
Sequence similarities	Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily. Contains 5 EGF-like domains. Contains 1 GPS domain.
Sequence caution	The sequence BAC06146.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	EGF-like domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Autocatalytic cleavage Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW neuropeptide signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Traceable author statement. Source: GDB plasma membrane Traceable author statement. Source: Reactome
Molecular function	G-protein coupled receptor activity Traceable author statement. Source: GDB calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: A number of isoforms are probably produced. A soluble form due to a frameshift which introduced a stop codon immediately before the first TM domain is also detected.

Isoform 1 (identifier: Q9UHX3-1)

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: Q9UHX3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     397-407: Missing.

Isoform 3 (identifier: Q9UHX3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     163-211: Missing.

Isoform 4 (identifier: Q9UHX3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     119-211: Missing.

Isoform 5 (identifier: Q9UHX3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     119-260: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Chain

24 – 823

800

EGF-like module-containing mucin-like hormone receptor-like 2

PRO_0000012875

Regions

Topological domain

24 – 540

517

Extracellular Potential

Transmembrane

541 – 561

21

Helical; Name=1; Potential

Topological domain

562 – 569

8

Cytoplasmic Potential

Transmembrane

570 – 590

21

Helical; Name=2; Potential

Topological domain

591 – 605

15

Extracellular Potential

Transmembrane

606 – 626

21

Helical; Name=3; Potential

Topological domain

627 – 644

18

Cytoplasmic Potential

Transmembrane

645 – 665

21

Helical; Name=4; Potential

Topological domain

666 – 683

18

Extracellular Potential

Transmembrane

684 – 704

21

Helical; Name=5; Potential

Topological domain

705 – 735

31

Cytoplasmic Potential

Transmembrane

736 – 756

21

Helical; Name=6; Potential

Topological domain

757 – 760

4

Extracellular Potential

Transmembrane

761 – 781

21

Helical; Name=7; Potential

Topological domain

782 – 823

42

Cytoplasmic Potential

Domain

25 – 66

42

EGF-like 1

Domain

67 – 118

52

EGF-like 2; calcium-binding

Domain

119 – 162

44

EGF-like 3; calcium-binding

Domain

163 – 211

49

EGF-like 4; calcium-binding Potential

Domain

212 – 260

49

EGF-like 5; calcium-binding Potential

Domain

479 – 529

51

GPS

Sites

Site

517 – 518

2

Cleavage

Amino acid modifications

Glycosylation

41

1

N-linked (GlcNAc...) Potential

Glycosylation

111

1

N-linked (GlcNAc...) Potential

Glycosylation

206

1

N-linked (GlcNAc...) Potential

Glycosylation

298

1

N-linked (GlcNAc...) Potential

Glycosylation

347

1

N-linked (GlcNAc...) Potential

Glycosylation

354

1

N-linked (GlcNAc...) Potential

Glycosylation

456

1

N-linked (GlcNAc...) Potential

Glycosylation

460

1

N-linked (GlcNAc...) Potential

Disulfide bond

29 ↔ 39

Ref.8

Disulfide bond

33 ↔ 45

Ref.8

Disulfide bond

47 ↔ 65

Ref.8

Disulfide bond

71 ↔ 85

Ref.8

Disulfide bond

79 ↔ 94

Ref.8

Disulfide bond

96 ↔ 117

Ref.8

Disulfide bond

123 ↔ 136

Ref.8

Disulfide bond

130 ↔ 145

Ref.8

Disulfide bond

147 ↔ 161

By similarity

Disulfide bond

167 ↔ 180

By similarity

Disulfide bond

174 ↔ 189

By similarity

Disulfide bond

191 ↔ 210

By similarity

Disulfide bond

216 ↔ 229

By similarity

Disulfide bond

223 ↔ 238

By similarity

Disulfide bond

240 ↔ 259

By similarity

Natural variations

Alternative sequence

119 – 260

142

Missing in isoform 5.

VSP_041364

Alternative sequence

119 – 211

93

Missing in isoform 4.

VSP_041365

Alternative sequence

163 – 211

49

Missing in isoform 3.

VSP_041366

Alternative sequence

397 – 407

11

Missing in isoform 2.

VSP_041367

Natural variant

314

1

A → V.
Corresponds to variant rs35612307 [ dbSNP | Ensembl ].

VAR_061229

Natural variant

605

1

T → I.
Corresponds to variant rs4410209 [ dbSNP | Ensembl ].

VAR_026719

Natural variant

614

1

L → F. Ref.1 Ref.3
Corresponds to variant rs2524383 [ dbSNP | Ensembl ].

VAR_026720

Natural variant

665

1

S → F.
Corresponds to variant rs3752187 [ dbSNP | Ensembl ].

VAR_026721

Natural variant

720

1

E → D.
Corresponds to variant rs57865820 [ dbSNP | Ensembl ].

VAR_061230

Experimental info

Mutagenesis

518

1

S → A: Abolishes cleavage. Ref.4

Sequence conflict

531

1

Missing in AAC05172. Ref.3

Sequence conflict

823

1

N → R in BAC06146. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

823

Helix Strand Turn

Details...

Beta strand

37 – 43

7

Beta strand

45 – 47

3

Beta strand

54 – 58

5

Helix

70 – 72

3

Beta strand

83 – 87

5

Beta strand

92 – 96

5

Beta strand

109 – 111

3

Helix

112 – 114

3

Beta strand

227 – 231

5

Beta strand

236 – 239

4

Beta strand

252 – 254

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 13, 2006. Version 2. Checksum: 4D38C30A07B46FF4	FASTA	823	90,472
	10 20 30 40 50 60 MGGRVFLVFL AFCVWLTLPG AETQDSRGCA RWCPQDSSCV NATACRCNPG FSSFSEIITT 70 80 90 100 110 120 PMETCDDINE CATLSKVSCG KFSDCWNTEG SYDCVCSPGY EPVSGAKTFK NESENTCQDV 130 140 150 160 170 180 DECQQNPRLC KSYGTCVNTL GSYTCQCLPG FKLKPEDPKL CTDVNECTSG QNPCHSSTHC 190 200 210 220 230 240 LNNVGSYQCR CRPGWQPIPG SPNGPNNTVC EDVDECSSGQ HQCDSSTVCF NTVGSYSCRC 250 260 270 280 290 300 RPGWKPRHGI PNNQKDTVCE DMTFSTWTPP PGVHSQTLSR FFDKVQDLGR DYKPGLANNT 310 320 330 340 350 360 IQSILQALDE LLEAPGDLET LPRLQQHCVA SHLLDGLEDV LRGLSKNLSN GLLNFSYPAG 370 380 390 400 410 420 TELSLEVQKQ VDRSVTLRQN QAVMQLDWNQ AQKSGDPGPS VVGLVSIPGM GKLLAEAPLV 430 440 450 460 470 480 LEPEKQMLLH ETHQGLLQDG SPILLSDVIS AFLSNNDTQN LSSPVTFTFS HRSVIPRQKV 490 500 510 520 530 540 LCVFWEHGQN GCGHWATTGC STIGTRDTST ICRCTHLSSF AVLMAHYDVQ EEDPVLTVIT 550 560 570 580 590 600 YMGLSVSLLC LLLAALTFLL CKAIQNTSTS LHLQLSLCLF LAHLLFLVAI DQTGHKVLCS 610 620 630 640 650 660 IIAGTLHYLY LATLTWMLLE ALYLFLTARN LTVVNYSSIN RFMKKLMFPV GYGVPAVTVA 670 680 690 700 710 720 ISAASRPHLY GTPSRCWLQP EKGFIWGFLG PVCAIFSVNL VLFLVTLWIL KNRLSSLNSE 730 740 750 760 770 780 VSTLRNTRML AFKATAQLFI LGCTWCLGIL QVGPAARVMA YLFTIINSLQ GVFIFLVYCL 790 800 810 820 LSQQVREQYG KWSKGIRKLK TESEMHTLSS SAKADTSKPS TVN
	Isoform 2 [UniParc]. Checksum: 9A98853A77E71FFD	FASTA	812	89,466
	10 20 30 40 50 60 MGGRVFLVFL AFCVWLTLPG AETQDSRGCA RWCPQDSSCV NATACRCNPG FSSFSEIITT 70 80 90 100 110 120 PMETCDDINE CATLSKVSCG KFSDCWNTEG SYDCVCSPGY EPVSGAKTFK NESENTCQDV 130 140 150 160 170 180 DECQQNPRLC KSYGTCVNTL GSYTCQCLPG FKLKPEDPKL CTDVNECTSG QNPCHSSTHC 190 200 210 220 230 240 LNNVGSYQCR CRPGWQPIPG SPNGPNNTVC EDVDECSSGQ HQCDSSTVCF NTVGSYSCRC 250 260 270 280 290 300 RPGWKPRHGI PNNQKDTVCE DMTFSTWTPP PGVHSQTLSR FFDKVQDLGR DYKPGLANNT 310 320 330 340 350 360 IQSILQALDE LLEAPGDLET LPRLQQHCVA SHLLDGLEDV LRGLSKNLSN GLLNFSYPAG 370 380 390 400 410 420 TELSLEVQKQ VDRSVTLRQN QAVMQLDWNQ AQKSGDPGMG KLLAEAPLVL EPEKQMLLHE 430 440 450 460 470 480 THQGLLQDGS PILLSDVISA FLSNNDTQNL SSPVTFTFSH RSVIPRQKVL CVFWEHGQNG 490 500 510 520 530 540 CGHWATTGCS TIGTRDTSTI CRCTHLSSFA VLMAHYDVQE EDPVLTVITY MGLSVSLLCL 550 560 570 580 590 600 LLAALTFLLC KAIQNTSTSL HLQLSLCLFL AHLLFLVAID QTGHKVLCSI IAGTLHYLYL 610 620 630 640 650 660 ATLTWMLLEA LYLFLTARNL TVVNYSSINR FMKKLMFPVG YGVPAVTVAI SAASRPHLYG 670 680 690 700 710 720 TPSRCWLQPE KGFIWGFLGP VCAIFSVNLV LFLVTLWILK NRLSSLNSEV STLRNTRMLA 730 740 750 760 770 780 FKATAQLFIL GCTWCLGILQ VGPAARVMAY LFTIINSLQG VFIFLVYCLL SQQVREQYGK 790 800 810 WSKGIRKLKT ESEMHTLSSS AKADTSKPST VN
	Isoform 3 [UniParc]. Checksum: 9687785185F52A7F	FASTA	774	85,230
	10 20 30 40 50 60 MGGRVFLVFL AFCVWLTLPG AETQDSRGCA RWCPQDSSCV NATACRCNPG FSSFSEIITT 70 80 90 100 110 120 PMETCDDINE CATLSKVSCG KFSDCWNTEG SYDCVCSPGY EPVSGAKTFK NESENTCQDV 130 140 150 160 170 180 DECQQNPRLC KSYGTCVNTL GSYTCQCLPG FKLKPEDPKL CTDVDECSSG QHQCDSSTVC 190 200 210 220 230 240 FNTVGSYSCR CRPGWKPRHG IPNNQKDTVC EDMTFSTWTP PPGVHSQTLS RFFDKVQDLG 250 260 270 280 290 300 RDYKPGLANN TIQSILQALD ELLEAPGDLE TLPRLQQHCV ASHLLDGLED VLRGLSKNLS 310 320 330 340 350 360 NGLLNFSYPA GTELSLEVQK QVDRSVTLRQ NQAVMQLDWN QAQKSGDPGP SVVGLVSIPG 370 380 390 400 410 420 MGKLLAEAPL VLEPEKQMLL HETHQGLLQD GSPILLSDVI SAFLSNNDTQ NLSSPVTFTF 430 440 450 460 470 480 SHRSVIPRQK VLCVFWEHGQ NGCGHWATTG CSTIGTRDTS TICRCTHLSS FAVLMAHYDV 490 500 510 520 530 540 QEEDPVLTVI TYMGLSVSLL CLLLAALTFL LCKAIQNTST SLHLQLSLCL FLAHLLFLVA 550 560 570 580 590 600 IDQTGHKVLC SIIAGTLHYL YLATLTWMLL EALYLFLTAR NLTVVNYSSI NRFMKKLMFP 610 620 630 640 650 660 VGYGVPAVTV AISAASRPHL YGTPSRCWLQ PEKGFIWGFL GPVCAIFSVN LVLFLVTLWI 670 680 690 700 710 720 LKNRLSSLNS EVSTLRNTRM LAFKATAQLF ILGCTWCLGI LQVGPAARVM AYLFTIINSL 730 740 750 760 770 QGVFIFLVYC LLSQQVREQY GKWSKGIRKL KTESEMHTLS SSAKADTSKP STVN
	Isoform 4 [UniParc]. Checksum: A7509F01725F3A18	FASTA	730	80,351
	10 20 30 40 50 60 MGGRVFLVFL AFCVWLTLPG AETQDSRGCA RWCPQDSSCV NATACRCNPG FSSFSEIITT 70 80 90 100 110 120 PMETCDDINE CATLSKVSCG KFSDCWNTEG SYDCVCSPGY EPVSGAKTFK NESENTCQDV 130 140 150 160 170 180 DECSSGQHQC DSSTVCFNTV GSYSCRCRPG WKPRHGIPNN QKDTVCEDMT FSTWTPPPGV 190 200 210 220 230 240 HSQTLSRFFD KVQDLGRDYK PGLANNTIQS ILQALDELLE APGDLETLPR LQQHCVASHL 250 260 270 280 290 300 LDGLEDVLRG LSKNLSNGLL NFSYPAGTEL SLEVQKQVDR SVTLRQNQAV MQLDWNQAQK 310 320 330 340 350 360 SGDPGPSVVG LVSIPGMGKL LAEAPLVLEP EKQMLLHETH QGLLQDGSPI LLSDVISAFL 370 380 390 400 410 420 SNNDTQNLSS PVTFTFSHRS VIPRQKVLCV FWEHGQNGCG HWATTGCSTI GTRDTSTICR 430 440 450 460 470 480 CTHLSSFAVL MAHYDVQEED PVLTVITYMG LSVSLLCLLL AALTFLLCKA IQNTSTSLHL 490 500 510 520 530 540 QLSLCLFLAH LLFLVAIDQT GHKVLCSIIA GTLHYLYLAT LTWMLLEALY LFLTARNLTV 550 560 570 580 590 600 VNYSSINRFM KKLMFPVGYG VPAVTVAISA ASRPHLYGTP SRCWLQPEKG FIWGFLGPVC 610 620 630 640 650 660 AIFSVNLVLF LVTLWILKNR LSSLNSEVST LRNTRMLAFK ATAQLFILGC TWCLGILQVG 670 680 690 700 710 720 PAARVMAYLF TIINSLQGVF IFLVYCLLSQ QVREQYGKWS KGIRKLKTES EMHTLSSSAK 730 ADTSKPSTVN
	Isoform 5 [UniParc]. Checksum: ADE8AC326340F0CB	FASTA	681	74,936
	10 20 30 40 50 60 MGGRVFLVFL AFCVWLTLPG AETQDSRGCA RWCPQDSSCV NATACRCNPG FSSFSEIITT 70 80 90 100 110 120 PMETCDDINE CATLSKVSCG KFSDCWNTEG SYDCVCSPGY EPVSGAKTFK NESENTCQDM 130 140 150 160 170 180 TFSTWTPPPG VHSQTLSRFF DKVQDLGRDY KPGLANNTIQ SILQALDELL EAPGDLETLP 190 200 210 220 230 240 RLQQHCVASH LLDGLEDVLR GLSKNLSNGL LNFSYPAGTE LSLEVQKQVD RSVTLRQNQA 250 260 270 280 290 300 VMQLDWNQAQ KSGDPGPSVV GLVSIPGMGK LLAEAPLVLE PEKQMLLHET HQGLLQDGSP 310 320 330 340 350 360 ILLSDVISAF LSNNDTQNLS SPVTFTFSHR SVIPRQKVLC VFWEHGQNGC GHWATTGCST 370 380 390 400 410 420 IGTRDTSTIC RCTHLSSFAV LMAHYDVQEE DPVLTVITYM GLSVSLLCLL LAALTFLLCK 430 440 450 460 470 480 AIQNTSTSLH LQLSLCLFLA HLLFLVAIDQ TGHKVLCSII AGTLHYLYLA TLTWMLLEAL 490 500 510 520 530 540 YLFLTARNLT VVNYSSINRF MKKLMFPVGY GVPAVTVAIS AASRPHLYGT PSRCWLQPEK 550 560 570 580 590 600 GFIWGFLGPV CAIFSVNLVL FLVTLWILKN RLSSLNSEVS TLRNTRMLAF KATAQLFILG 610 620 630 640 650 660 CTWCLGILQV GPAARVMAYL FTIINSLQGV FIFLVYCLLS QQVREQYGKW SKGIRKLKTE 670 680 SEMHTLSSSA KADTSKPSTV N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human EMR2, a novel EGF-TM7 molecule on chromosome 19p13.1, is closely related to CD97." Lin H.-H., Stacey M., Hamann J., Gordon S., McKnight A.J. Genomics 67:188-200(2000) [PubMed: 10903844] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 2; 3; 4 AND 5), VARIANT PHE-614.
[2]	"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes." Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-614.
[4]	"Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif." Chang G.-W., Stacey M., Kwakkenbos M.J., Hamann J., Gordon S., Lin H.-H. FEBS Lett. 547:145-150(2003) [PubMed: 12860403] [Abstract] Cited for: PROTEIN SEQUENCE OF 518-527, PROTEOLYTIC PROCESSING, MUTAGENESIS OF SER-518.
[5]	"The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans." Stacey M., Chang G.-W., Davies J.Q., Kwakkenbos M.J., Sanderson R.D., Hamann J., Gordon S., Lin H.-H. Blood 102:2916-2924(2003) [PubMed: 12829604] [Abstract] Cited for: INTERACTION WITH CHONDROITIN SULFATE.
[6]	"The human EGF-TM7 family member EMR2 is a heterodimeric receptor expressed on myeloid cells." Kwakkenbos M.J., Chang G.-W., Lin H.-H., Pouwels W., de Jong E.C., van Lier R.A.W., Gordon S., Hamann J. J. Leukoc. Biol. 71:854-862(2002) [PubMed: 11994511] [Abstract] Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
[7]	"Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif." Lin H.H., Chang G.W., Davies J.Q., Stacey M., Harris J., Gordon S. J. Biol. Chem. 279:31823-31832(2004) [PubMed: 15150276] [Abstract] Cited for: AUTOPROTEOLYTIC CLEAVAGE, SUBUNIT.
[8]	"Structural and functional characterization of a novel T cell receptor co-regulatory protein complex, CD97-CD55." Abbott R.J., Spendlove I., Roversi P., Fitzgibbon H., Knott V., Teriete P., McDonnell J.M., Handford P.A., Lea S.M. J. Biol. Chem. 282:22023-22032(2007) [PubMed: 17449467] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-152, CALCIUM-BINDING, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF114491 mRNA. Translation: AAF21974.1.
AB065931 Genomic DNA. Translation: BAC06146.1. Sequence problems.
AC004262 Genomic DNA. Translation: AAC05172.1.
AC005327 Genomic DNA. No translation available.
AC090427 Genomic DNA. No translation available.

IPI

IPI00183280.
IPI00183838.
IPI00296277.
IPI00375382.
IPI00549702.

RefSeq

NP_038475.2. NM_013447.2.
NP_690880.1. NM_152916.1.
NP_690881.1. NM_152917.1.
NP_690882.1. NM_152918.1.
NP_690883.1. NM_152919.1.
NP_690884.1. NM_152920.1.
NP_690885.1. NM_152921.1.

UniGene

Hs.531619.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BO2	X-ray	2.60	A/B	25-260	[»]
2BOU	X-ray	1.90	A	25-260	[»]
2BOX	X-ray	2.50	A	25-260	[»]

ProteinModelPortal

Q9UHX3.

SMR

Q9UHX3. Positions 28-260.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9UHX3.

Protein family/group databases

MEROPS

S63.001.

GPCRDB

Search...

Polymorphism databases

DMDM

108935835.

Proteomic databases

PRIDE

Q9UHX3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000315576; ENSP00000319883; ENSG00000127507.

GeneID

30817.

KEGG

hsa:30817.

UCSC

uc002mzp.1. human.

Organism-specific databases

CTD

30817.

GeneCards

GC19M014844.

H-InvDB

HIX0014843.

HGNC

HGNC:3337. EMR2.

MIM

606100. gene.

neXtProt

NX_Q9UHX3.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00600000084176.

HOGENOM

HBG506068.

HOVERGEN

HBG048917.

InParanoid

Q9UHX3.

PhylomeDB

Q9UHX3.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q9UHX3.

Bgee

Q9UHX3.

CleanEx

HS_EMR2.

Genevestigator

Q9UHX3.

GermOnline

ENSG00000127507. Homo sapiens.

Family and domain databases

InterPro

IPR001881. EGF-like_Ca-bd.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000742. EGF_3.
IPR018097. EGF_Ca-bd_CS.
IPR017981. GPCR_2-like.
IPR003056. GPCR_2_CD97.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS_dom.
[Graphical view]

KO

K08443.

Pfam

PF00002. 7tm_2. 1 hit.
PF07645. EGF_CA. 4 hits.
PF01825. GPS. 1 hit.
[Graphical view]

PRINTS

PR01278. CD97PROTEIN.
PR00249. GPCRSECRETIN.

SMART

SM00179. EGF_CA. 4 hits.
SM00303. GPS. 1 hit.
[Graphical view]

PROSITE

PS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. False negative.
PS01186. EGF_2. False negative.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 4 hits.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

52882.

PMAP-CutDB

Q9UHX3.

SOURCE

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Entry information

Entry name

EMR2_HUMAN

Accession

Primary (citable) accession number: Q9UHX3
Secondary accession number(s): E9PBR1 , E9PEL6, E9PFQ5, E9PG91, Q8NG96, Q9Y4B1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	June 13, 2006
Last modified:	January 25, 2012
This is version 114 of the entry and version 2 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.