ID   AGRE5_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   24-JAN-2024, entry version 184.
DE   RecName: Full=Adhesion G protein-coupled receptor E5 {ECO:0000312|MGI:MGI:1347095};
DE   AltName: Full=Leukocyte antigen CD97 {ECO:0000250|UniProtKB:P48960};
DE   AltName: CD_antigen=CD97;
DE   Contains:
DE     RecName: Full=Adhesion G protein-coupled receptor E5 subunit alpha;
DE   Contains:
DE     RecName: Full=Adhesion G protein-coupled receptor E5 subunit beta;
DE   Flags: Precursor;
GN   Name=Adgre5 {ECO:0000312|MGI:MGI:1347095};
GN   Synonyms=Cd97 {ECO:0000312|MGI:MGI:1347095};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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, AND
RP   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 project:
RT   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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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 CD97 is
RT   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 AND ASN-461.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., 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 AND ASN-395.
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-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-814, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Receptor potentially involved in both adhesion and signaling
CC       processes early after leukocyte activation. Plays an essential role in
CC       leukocyte migration. {ECO:0000269|PubMed:14707087}.
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region (alpha subunit) non-covalently linked to a seven-transmembrane
CC       moiety (beta subunit). Interacts with complement decay-accelerating
CC       factor (DAF). The largest isoform (isoform 1) do not interact with DAF.
CC       Interacts also with chondroitin sulfate (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10540231};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor E5 subunit
CC       alpha]: Secreted, extracellular space {ECO:0000305}.
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 the
CC       immune system, expressed ubiquitously with particularly high levels of
CC       expression in the lung and the thymus gland. In the spleen, expression
CC       is detected on most myeloid cells and variable portions of T-cells, B-
CC       cells and NK cells. In the bone marrow, expressed in nearly all myeloid
CC       cells, whereas little if any expression is found on erythroid cells.
CC   -!- INDUCTION: Up-regulated during lymphocyte activation.
CC   -!- DOMAIN: The first two EGF domains mediate the interaction with DAF. A
CC       third tandemly arranged EGF domain is necessary for the structural
CC       integrity of the binding region (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: Binding to chondroitin sulfate is mediated by the fourth EGF
CC       domain. {ECO:0000250}.
CC   -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha
CC       subunit and a seven-transmembrane subunit. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC       subfamily. {ECO:0000305}.
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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   AlphaFoldDB; Q9Z0M6; -.
DR   SMR; Q9Z0M6; -.
DR   BioGRID; 204924; 13.
DR   STRING; 10090.ENSMUSP00000075240; -.
DR   MEROPS; P02.033; -.
DR   GlyCosmos; Q9Z0M6; 7 sites, No reported glycans.
DR   GlyGen; Q9Z0M6; 7 sites.
DR   iPTMnet; Q9Z0M6; -.
DR   PhosphoSitePlus; Q9Z0M6; -.
DR   CPTAC; non-CPTAC-3898; -.
DR   EPD; Q9Z0M6; -.
DR   MaxQB; Q9Z0M6; -.
DR   PaxDb; 10090-ENSMUSP00000075240; -.
DR   ProteomicsDB; 265634; -. [Q9Z0M6-1]
DR   ProteomicsDB; 265635; -. [Q9Z0M6-2]
DR   ProteomicsDB; 265636; -. [Q9Z0M6-3]
DR   Pumba; Q9Z0M6; -.
DR   DNASU; 26364; -.
DR   GeneID; 26364; -.
DR   KEGG; mmu:26364; -.
DR   AGR; MGI:1347095; -.
DR   CTD; 976; -.
DR   MGI; MGI:1347095; Adgre5.
DR   eggNOG; KOG4193; Eukaryota.
DR   InParanoid; Q9Z0M6; -.
DR   OrthoDB; 1114672at2759; -.
DR   PhylomeDB; Q9Z0M6; -.
DR   Reactome; R-MMU-373080; Class B/2 (Secretin family receptors).
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 26364; 1 hit in 77 CRISPR screens.
DR   PRO; PR:Q9Z0M6; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9Z0M6; Protein.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031256; C:leading edge membrane; ISO:MGI.
DR   GO; GO:0016020; C:membrane; TAS:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0035374; F:chondroitin sulfate binding; ISO:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:MGI.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR   CDD; cd00054; EGF_CA; 3.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR003056; GPCR_2_ADGRE2_ADGRE5.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS.
DR   PANTHER; PTHR12011:SF348; ADHESION G PROTEIN-COUPLED RECEPTOR E5; 1.
DR   PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
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; 4.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00303; GPS; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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   Disulfide bond; EGF-like domain; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted;
KW   Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..818
FT                   /note="Adhesion G protein-coupled receptor E5"
FT                   /id="PRO_0000012869"
FT   CHAIN           24..513
FT                   /note="Adhesion G protein-coupled receptor E5 subunit
FT                   alpha"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000435126"
FT   CHAIN           514..818
FT                   /note="Adhesion G protein-coupled receptor E5 subunit beta"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000435127"
FT   TOPO_DOM        24..533
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        534..554
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        555..562
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        563..583
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        584..602
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        603..623
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        624..637
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        638..658
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        659..679
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        680..700
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        701..723
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        724..744
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        745..752
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        753..773
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        774..818
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..68
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          69..119
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          165..213
FT                   /note="EGF-like 3; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          214..261
FT                   /note="EGF-like 4; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          479..524
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          799..818
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            513..514
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         798
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48960"
FT   MOD_RES         808
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P48960"
FT   MOD_RES         814
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         816
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48960"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973,
FT                   ECO:0000269|PubMed:19656770"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        35..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        49..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        73..86
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        80..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        97..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        169..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        176..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        193..212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        218..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        225..240
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        242..260
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VAR_SEQ         120..213
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10540231,
FT                   ECO:0000303|PubMed:10744645, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009413"
FT   VAR_SEQ         120..164
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10540231,
FT                   ECO:0000303|PubMed:10744645"
FT                   /id="VSP_009414"
FT   CONFLICT        3
FT                   /note="G -> S (in Ref. 1; CAB38246)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        28
FT                   /note="S -> I (in Ref. 1; CAB38246)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="Q -> E (in Ref. 3; AAH06676)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        506
FT                   /note="F -> S (in Ref. 2; AAF67800)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        599
FT                   /note="M -> V (in Ref. 3; AAH06676)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        726
FT                   /note="A -> S (in Ref. 3 and 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        796
FT                   /note="F -> I (in Ref. 4; BAB25461)"
FT                   /evidence="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
//