ID CD97_MOUSE Reviewed; 818 AA.
AC Q9Z0M6; Q923A1; Q9CVI5; Q9JLQ8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 01-MAY-2013, entry version 113.
DE RecName: Full=CD97 antigen;
DE AltName: CD_antigen=CD97;
DE Flags: Precursor;
GN Name=Cd97;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=10744645; DOI=10.1093/intimm/12.4.439;
RA Hamann J., van Zventer C., Bijl A., Molenaar C., Tesselaar K.,
RA van Lier R.A.W.;
RT "Molecular cloning and characterization of mouse CD97.";
RL Int. Immunol. 12:439-448(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INTERACTION WITH DAF,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=10540231; DOI=10.1046/j.1365-2567.1999.00859.x;
RA Qian Y.-M., Haino M., Kelly K., Song W.-C.;
RT "Structural characterization of mouse CD97 and study of its specific
RT interaction with the murine decay-accelerating factor (DAF, CD55).";
RL Immunology 98:303-311(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 607-818.
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION.
RX PubMed=14707087;
RA Leemans J.C., te Velde A.A., Florquin S., Bennink R.J., de Bruin K.,
RA van Lier R.A.W., van der Poll T., Hamann J.;
RT "The epidermal growth factor-seven transmembrane (EGF-TM7) receptor
RT CD97 is required for neutrophil migration and host defense.";
RL J. Immunol. 172:1125-1131(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299; ASN-395; ASN-407 AND
RP ASN-461, AND MASS SPECTROMETRY.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299; ASN-395 AND ASN-407,
RP AND MASS SPECTROMETRY.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: Receptor potentially involved in both adhesion and
CC signaling processes early after leukocyte activation. Plays an
CC essential role in leukocyte migration.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region (alpha subunit) non-covalently linked to a seven-
CC transmembrane moiety (beta subunit). Interacts with complement
CC decay-accelerating factor (DAF). The largest isoform (isoform 1)
CC do not interact with DAF. Interacts also with chondroitin sulfate
CC (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=EGF(1,2,X,3,4);
CC IsoId=Q9Z0M6-1; Sequence=Displayed;
CC Name=2; Synonyms=EGF(1,2,4);
CC IsoId=Q9Z0M6-2; Sequence=VSP_009413;
CC Name=3; Synonyms=EGF(1,2,3,4);
CC IsoId=Q9Z0M6-3; Sequence=VSP_009414;
CC -!- TISSUE SPECIFICITY: Although predominantly expressed by cells of
CC the immune system is expressed ubiquitously, with particularly
CC high levels of expression in the lung and the thymus gland. In the
CC spleen, expression is detected on most myeloid cells and variable
CC portions of T-cells, B-cells and NK cells. In the bone marrow,
CC expressed in nearly all myeloid cells, whereas little if any
CC expression is found on erythroid cells.
CC -!- INDUCTION: Up-regulated during lymphocyte activation.
CC -!- DOMAIN: The first two EGF domains mediate the interaction with
CC DAF. A third tandemly arranged EGF domain is necessary for the
CC structural integrity of the binding region (By similarity).
CC -!- DOMAIN: Binding to chondroitin sulfate is mediated by the fourth
CC EGF domain (By similarity).
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
CC alpha subunit and a seven-transmembrane subunit (By similarity).
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC LN-TM7 subfamily.
CC -!- SIMILARITY: Contains 4 EGF-like domains.
CC -!- SIMILARITY: Contains 1 GPS domain.
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DR EMBL; Y18365; CAB38246.1; -; mRNA.
DR EMBL; AF146344; AAF67800.1; -; mRNA.
DR EMBL; BC006676; AAH06676.1; -; mRNA.
DR EMBL; AK008101; BAB25461.1; -; mRNA.
DR IPI; IPI00399798; -.
DR IPI; IPI00399799; -.
DR IPI; IPI00399800; -.
DR RefSeq; NP_001156501.1; NM_001163029.1.
DR UniGene; Mm.334648; -.
DR ProteinModelPortal; Q9Z0M6; -.
DR SMR; Q9Z0M6; 31-261.
DR STRING; 10090.ENSMUSP00000075240; -.
DR MEROPS; S63.036; -.
DR PhosphoSite; Q9Z0M6; -.
DR PaxDb; Q9Z0M6; -.
DR PRIDE; Q9Z0M6; -.
DR Ensembl; ENSMUST00000002964; ENSMUSP00000002964; ENSMUSG00000002885.
DR GeneID; 26364; -.
DR KEGG; mmu:26364; -.
DR UCSC; uc009mlc.2; mouse.
DR UCSC; uc012ggt.1; mouse.
DR CTD; 976; -.
DR MGI; MGI:1347095; Cd97.
DR eggNOG; NOG320737; -.
DR GeneTree; ENSGT00650000093107; -.
DR HOGENOM; HOG000294115; -.
DR HOVERGEN; HBG048917; -.
DR InParanoid; Q9Z0M6; -.
DR KO; K08446; -.
DR OrthoDB; EOG45X7WF; -.
DR ChiTaRS; CD97; mouse.
DR NextBio; 304231; -.
DR ArrayExpress; Q9Z0M6; -.
DR Bgee; Q9Z0M6; -.
DR CleanEx; MM_CD97; -.
DR Genevestigator; Q9Z0M6; -.
DR GermOnline; ENSMUSG00000002885; Mus musculus.
DR GO; GO:0016021; C:integral to membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR InterPro; IPR000742; EG-like_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003056; GPCR_2_CD97.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS_dom.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR01278; CD97PROTEIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Complete proteome; Disulfide bond; EGF-like domain;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 23 Potential.
FT CHAIN 24 818 CD97 antigen.
FT /FTId=PRO_0000012869.
FT TOPO_DOM 24 533 Extracellular (Potential).
FT TRANSMEM 534 554 Helical; Name=1; (Potential).
FT TOPO_DOM 555 562 Cytoplasmic (Potential).
FT TRANSMEM 563 583 Helical; Name=2; (Potential).
FT TOPO_DOM 584 602 Extracellular (Potential).
FT TRANSMEM 603 623 Helical; Name=3; (Potential).
FT TOPO_DOM 624 637 Cytoplasmic (Potential).
FT TRANSMEM 638 658 Helical; Name=4; (Potential).
FT TOPO_DOM 659 679 Extracellular (Potential).
FT TRANSMEM 680 700 Helical; Name=5; (Potential).
FT TOPO_DOM 701 723 Cytoplasmic (Potential).
FT TRANSMEM 724 744 Helical; Name=6; (Potential).
FT TOPO_DOM 745 752 Extracellular (Potential).
FT TRANSMEM 753 773 Helical; Name=7; (Potential).
FT TOPO_DOM 774 818 Cytoplasmic (Potential).
FT DOMAIN 27 68 EGF-like 1.
FT DOMAIN 69 119 EGF-like 2; calcium-binding (Potential).
FT DOMAIN 165 213 EGF-like 3; calcium-binding (Potential).
FT DOMAIN 214 261 EGF-like 4; calcium-binding (Potential).
FT DOMAIN 479 524 GPS.
FT SITE 513 514 Cleavage (By similarity).
FT MOD_RES 814 814 Phosphoserine (By similarity).
FT MOD_RES 816 816 Phosphoserine (By similarity).
FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 112 112 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 227 227 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 299 299 N-linked (GlcNAc...).
FT CARBOHYD 395 395 N-linked (GlcNAc...).
FT CARBOHYD 407 407 N-linked (GlcNAc...).
FT CARBOHYD 461 461 N-linked (GlcNAc...).
FT CARBOHYD 502 502 N-linked (GlcNAc...) (Potential).
FT DISULFID 31 41 By similarity.
FT DISULFID 35 47 By similarity.
FT DISULFID 49 67 By similarity.
FT DISULFID 73 86 By similarity.
FT DISULFID 80 95 By similarity.
FT DISULFID 97 118 By similarity.
FT DISULFID 169 182 By similarity.
FT DISULFID 176 191 By similarity.
FT DISULFID 193 212 By similarity.
FT DISULFID 218 231 By similarity.
FT DISULFID 225 240 By similarity.
FT DISULFID 242 260 By similarity.
FT VAR_SEQ 120 213 Missing (in isoform 2).
FT /FTId=VSP_009413.
FT VAR_SEQ 120 164 Missing (in isoform 3).
FT /FTId=VSP_009414.
FT CONFLICT 3 3 G -> S (in Ref. 1; CAB38246).
FT CONFLICT 28 28 S -> I (in Ref. 1; CAB38246).
FT CONFLICT 320 320 Q -> E (in Ref. 3; AAH06676).
FT CONFLICT 506 506 F -> S (in Ref. 2; AAF67800).
FT CONFLICT 599 599 M -> V (in Ref. 3; AAH06676).
FT CONFLICT 726 726 A -> S (in Ref. 3 and 4).
FT CONFLICT 796 796 F -> I (in Ref. 4; BAB25461).
SQ SEQUENCE 818 AA; 90413 MW; E59A292F2CF626C2 CRC64;
MRGVRCPGLL VVCILLSLSG AGTQKAESKN CAKWCPINSK CVSNRSCVCK PGFSSEKELI
TNPAESCEDI NECLLPGFSC GDFAMCKNSE GSYTCVCNLG YKLLSGAESF VNESENTCQA
SVNTGTTPVP SRIHTVTTAP GNLPEQTTTV HQTQMGDSEE RTPKDVNECI SGQNHCHQST
HCINKLGGYS CICRQGWKPV PGSPNGPVST VCEDVDECSS GQHQCHNSTV CKNTVGSYKC
HCRPGWKPTS GSLRGPDTIC QEPPFPTWTL LPTAHSQTLL RFSVEVQNLL RDFNPATVNY
TIQKLIEAVD KLLEDPMETQ TQQVAAQLLS NLEQSLRTLA QFLPKGPFTY TSPSNTELSL
MVKEQDNKDV TTVHHGQTWM ELDWAVTAGA KISENGSSVA GILSSPNMEK LLGNTPLNLE
QRRASLEDFY GSPIPSVSLK LLSNINSVFL TNTNTEKLAS NVTFKFDFTS VESIEPRHEL
ICAFWKAHNG NGYWDTDGCS MNGTGFCHCN HLTSFAILMA QYHVQDPRLE LITKVGLLLS
LICLLLCILT FLLVKPIQSS RTMVHLHLCI CLFLGSIIFL VGVENEGGEV GLRCRLVAMM
LHFCFLAAFC WMALEGVELY FLVVRVFQGQ GLSTWQRCLI GYGVPLLIVA ISMAVVKMDG
YGHATYCWLD FRKQGFLWSF SGPVAFIIFC NAAIFVITVW KLTKKFSEIN PNMKKLRKAR
VLTITAIAQL LVLGCTWGFG LFLFNPHSTW LSYIFTLLNC LQGLFLYVML CLLNKKVREE
YWKWACMVTG SKYTEFNSST TGTGTSQTRA LRSSESGM
//
