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Database: UniProt
Entry: Q9Z0M6
LinkDB: Q9Z0M6
Original site: Q9Z0M6 
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-OCT-2014, entry version 127.
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; DOI=10.4049/jimmunol.172.2.1125;
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.
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.
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       {ECO:0000269|PubMed:14707087}.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10540231};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:10540231}.
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       {ECO:0000250}.
CC   -!- DOMAIN: Binding to chondroitin sulfate is mediated by the fourth
CC       EGF domain. {ECO:0000250}.
CC   -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
CC       alpha subunit and a seven-transmembrane subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 4 EGF-like domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
CC   -!- SIMILARITY: Contains 1 GPS domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00098}.
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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   CCDS; CCDS22461.1; -. [Q9Z0M6-1]
DR   CCDS; CCDS52610.1; -. [Q9Z0M6-2]
DR   CCDS; CCDS52611.1; -. [Q9Z0M6-3]
DR   RefSeq; NP_001156501.1; NM_001163029.1.
DR   UniGene; Mm.334648; -.
DR   ProteinModelPortal; Q9Z0M6; -.
DR   SMR; Q9Z0M6; 31-261, 557-780.
DR   IntAct; Q9Z0M6; 1.
DR   MINT; MINT-4090290; -.
DR   STRING; 10090.ENSMUSP00000075240; -.
DR   MEROPS; S63.036; -.
DR   PhosphoSite; Q9Z0M6; -.
DR   MaxQB; Q9Z0M6; -.
DR   PaxDb; Q9Z0M6; -.
DR   PRIDE; Q9Z0M6; -.
DR   Ensembl; ENSMUST00000002964; ENSMUSP00000002964; ENSMUSG00000002885.
DR   GeneID; 26364; -.
DR   KEGG; mmu:26364; -.
DR   CTD; 976; -.
DR   MGI; MGI:1347095; Cd97.
DR   eggNOG; NOG320737; -.
DR   GeneTree; ENSGT00710000106562; -.
DR   HOGENOM; HOG000294115; -.
DR   HOVERGEN; HBG048917; -.
DR   InParanoid; Q9Z0M6; -.
DR   KO; K08446; -.
DR   OrthoDB; EOG75J0MK; -.
DR   PhylomeDB; Q9Z0M6; -.
DR   ChiTaRS; CD97; mouse.
DR   NextBio; 304231; -.
DR   PRO; PR:Q9Z0M6; -.
DR   ArrayExpress; Q9Z0M6; -.
DR   Bgee; Q9Z0M6; -.
DR   CleanEx; MM_CD97; -.
DR   Genevestigator; Q9Z0M6; -.
DR   GO; GO:0016021; C:integral component of 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_dom.
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.
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; 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       {ECO:0000255}.
FT   CHAIN        24    818       CD97 antigen.
FT                                /FTId=PRO_0000012869.
FT   TOPO_DOM     24    533       Extracellular. {ECO:0000255}.
FT   TRANSMEM    534    554       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM    555    562       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    563    583       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    584    602       Extracellular. {ECO:0000255}.
FT   TRANSMEM    603    623       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    624    637       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    638    658       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    659    679       Extracellular. {ECO:0000255}.
FT   TRANSMEM    680    700       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    701    723       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    724    744       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    745    752       Extracellular. {ECO:0000255}.
FT   TRANSMEM    753    773       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    774    818       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       27     68       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       69    119       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      165    213       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      214    261       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      479    524       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   SITE        513    514       Cleavage. {ECO:0000250}.
FT   MOD_RES     814    814       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     816    816       Phosphoserine. {ECO:0000250}.
FT   CARBOHYD     44     44       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    112    112       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    227    227       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    299    299       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:19656770}.
FT   CARBOHYD    395    395       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:19656770}.
FT   CARBOHYD    407    407       N-linked (GlcNAc...); atypical.
FT                                {ECO:0000269|PubMed:19349973,
FT                                ECO:0000269|PubMed:19656770}.
FT   CARBOHYD    461    461       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:19656770}.
FT   CARBOHYD    502    502       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     31     41       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     35     47       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     49     67       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     73     86       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     80     95       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     97    118       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    169    182       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    176    191       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    193    212       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    218    231       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    225    240       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    242    260       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     120    213       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10540231,
FT                                ECO:0000303|PubMed:10744645,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_009413.
FT   VAR_SEQ     120    164       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:10540231,
FT                                ECO:0000303|PubMed:10744645}.
FT                                /FTId=VSP_009414.
FT   CONFLICT      3      3       G -> S (in Ref. 1; CAB38246).
FT                                {ECO:0000305}.
FT   CONFLICT     28     28       S -> I (in Ref. 1; CAB38246).
FT                                {ECO:0000305}.
FT   CONFLICT    320    320       Q -> E (in Ref. 3; AAH06676).
FT                                {ECO:0000305}.
FT   CONFLICT    506    506       F -> S (in Ref. 2; AAF67800).
FT                                {ECO:0000305}.
FT   CONFLICT    599    599       M -> V (in Ref. 3; AAH06676).
FT                                {ECO:0000305}.
FT   CONFLICT    726    726       A -> S (in Ref. 3 and 4). {ECO:0000305}.
FT   CONFLICT    796    796       F -> I (in Ref. 4; BAB25461).
FT                                {ECO:0000305}.
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
//
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