ID AGRB2_MOUSE Reviewed; 1561 AA.
AC Q8CGM1; B1ASB7; B1ASB8; B2FDE3; Q3TYC8; Q3UN11; Q3UNE2; Q6PGN0;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Adhesion G protein-coupled receptor B2;
DE AltName: Full=Brain-specific angiogenesis inhibitor 2;
DE Flags: Precursor;
GN Name=Adgrb2; Synonyms=Bai2;
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] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND FUNCTION.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=12218411; DOI=10.1097/00004647-200209000-00003;
RA Kee H.J., Koh J.T., Kim M.Y., Ahn K.Y., Kim J.K., Bae C.S., Park S.S.,
RA Kim K.K.;
RT "Expression of brain-specific angiogenesis inhibitor 2 (BAI2) in normal and
RT ischemic brain: involvement of BAI2 in the ischemia-induced brain
RT angiogenesis.";
RL J. Cereb. Blood Flow Metab. 22:1054-1067(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Visual cortex;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP INTERACTION WITH GABPB2.
RX PubMed=16412436; DOI=10.1016/j.febslet.2005.12.086;
RA Jeong B.C., Kim M.Y., Lee J.H., Kee H.J., Kho D.H., Han K.E., Qian Y.R.,
RA Kim J.K., Kim K.K.;
RT "Brain-specific angiogenesis inhibitor 2 regulates VEGF through GABP that
RT acts as a transcriptional repressor.";
RL FEBS Lett. 580:669-676(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1345, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=21110148; DOI=10.1007/s12576-010-0120-0;
RA Okajima D., Kudo G., Yokota H.;
RT "Antidepressant-like behavior in brain-specific angiogenesis inhibitor 2-
RT deficient mice.";
RL J. Physiol. Sci. 61:47-54(2011).
RN [9]
RP INTERACTION WITH SH3GL2.
RX PubMed=28891236; DOI=10.1002/humu.23336;
RA Purcell R.H., Toro C., Gahl W.A., Hall R.A.;
RT "A disease-associated mutation in the adhesion GPCR BAI2 (ADGRB2) increases
RT receptor signaling activity.";
RL Hum. Mutat. 38:1751-1760(2017).
CC -!- FUNCTION: Orphan G-protein coupled receptor involved in cell adhesion
CC and probably in cell-cell interactions. Activates NFAT-signaling
CC pathway, a transcription factor, via the G-protein GNAZ. Involved in
CC angiogenesis inhibition (PubMed:12218411).
CC {ECO:0000250|UniProtKB:O60241, ECO:0000269|PubMed:12218411}.
CC -!- ACTIVITY REGULATION: Receptor activity is regulated by proteolytic
CC processing. The long N-terminal has a an inhibitory effect on the
CC constitutive signaling activity. Removal of the N-terminal region
CC induces an increase of the receptor activity.
CC {ECO:0000250|UniProtKB:O60241}.
CC -!- SUBUNIT: Heterodimer of 2 chains generated by proteolytic processing;
CC the large extracellular N-terminal fragment and the membrane-bound C-
CC terminal fragment predominantly remain associated and non-covalently
CC linked. Interacts with GABPB2 (PubMed:16412436). Interacts (via
CC carboxy-terminus) with TAX1BP3. Interacts with GNAZ (By similarity).
CC Interacts with SH3GL2 (PubMed:28891236). {ECO:0000250|UniProtKB:O60241,
CC ECO:0000269|PubMed:16412436, ECO:0000269|PubMed:28891236}.
CC -!- INTERACTION:
CC Q8CGM1; Q06547: GABPB1; Xeno; NbExp=3; IntAct=EBI-8014984, EBI-618165;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60241};
CC Multi-pass membrane protein {ECO:0000255}. Secreted
CC {ECO:0000250|UniProtKB:O60241}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CGM1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CGM1-2; Sequence=VSP_019762;
CC Name=3;
CC IsoId=Q8CGM1-3; Sequence=VSP_019763;
CC -!- TISSUE SPECIFICITY: Specifically expressed in the brain. The peak level
CC in the brain is observed 10 days after birth.
CC {ECO:0000269|PubMed:12218411}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitous in embryonic tissues, but expression is
CC acutely down-regulated after birth, except in the brain, to a level
CC that is maintained throughout adulthood. {ECO:0000269|PubMed:12218411}.
CC -!- INDUCTION: Down-regulated after hypoxia.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:O60241}.
CC -!- PTM: Autoproteolytically processed at the GPS domain; this cleavage
CC modulates receptor activity. Additionally, furin is involved in the
CC cleavage at another site, in the middle of the extracellular domain,
CC generating a soluble fragment. {ECO:0000250|UniProtKB:O60241}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice show significant resistance to
CC depression after repeated stress in the social defeat test.
CC Additionally, hippocampal cell proliferation in deficient mice is
CC increased. {ECO:0000269|PubMed:21110148}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR EMBL; AY168407; AAN86965.1; -; mRNA.
DR EMBL; AK144268; BAE25805.1; -; mRNA.
DR EMBL; AK144559; BAE25937.1; -; mRNA.
DR EMBL; AK158735; BAE34635.1; -; mRNA.
DR EMBL; AL626774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056926; AAH56926.1; -; mRNA.
DR CCDS; CCDS51309.1; -. [Q8CGM1-3]
DR CCDS; CCDS57300.1; -. [Q8CGM1-2]
DR CCDS; CCDS80164.1; -. [Q8CGM1-1]
DR RefSeq; NP_001186625.1; NM_001199696.1. [Q8CGM1-2]
DR RefSeq; NP_001277643.1; NM_001290714.1.
DR RefSeq; NP_001277644.1; NM_001290715.1. [Q8CGM1-1]
DR RefSeq; NP_775094.2; NM_173071.3. [Q8CGM1-3]
DR AlphaFoldDB; Q8CGM1; -.
DR SMR; Q8CGM1; -.
DR BioGRID; 231022; 8.
DR IntAct; Q8CGM1; 5.
DR MINT; Q8CGM1; -.
DR STRING; 10090.ENSMUSP00000101636; -.
DR MEROPS; P02.029; -.
DR GlyConnect; 2108; 8 N-Linked glycans (2 sites).
DR GlyCosmos; Q8CGM1; 8 sites, 8 glycans.
DR GlyGen; Q8CGM1; 9 sites, 8 N-linked glycans (2 sites).
DR iPTMnet; Q8CGM1; -.
DR PhosphoSitePlus; Q8CGM1; -.
DR SwissPalm; Q8CGM1; -.
DR MaxQB; Q8CGM1; -.
DR PaxDb; 10090-ENSMUSP00000101638; -.
DR ProteomicsDB; 296126; -. [Q8CGM1-1]
DR ProteomicsDB; 296127; -. [Q8CGM1-2]
DR ProteomicsDB; 296128; -. [Q8CGM1-3]
DR Antibodypedia; 16794; 330 antibodies from 33 providers.
DR DNASU; 230775; -.
DR Ensembl; ENSMUST00000106015.9; ENSMUSP00000101636.3; ENSMUSG00000028782.15. [Q8CGM1-1]
DR Ensembl; ENSMUST00000106017.8; ENSMUSP00000101638.2; ENSMUSG00000028782.15. [Q8CGM1-3]
DR Ensembl; ENSMUST00000121049.8; ENSMUSP00000112869.2; ENSMUSG00000028782.15. [Q8CGM1-2]
DR GeneID; 230775; -.
DR KEGG; mmu:230775; -.
DR UCSC; uc008uym.3; mouse. [Q8CGM1-3]
DR UCSC; uc008uyn.3; mouse. [Q8CGM1-2]
DR UCSC; uc008uyp.1; mouse. [Q8CGM1-1]
DR AGR; MGI:2451244; -.
DR CTD; 576; -.
DR MGI; MGI:2451244; Adgrb2.
DR VEuPathDB; HostDB:ENSMUSG00000028782; -.
DR eggNOG; ENOG502QRKJ; Eukaryota.
DR GeneTree; ENSGT00940000160103; -.
DR HOGENOM; CLU_003751_1_0_1; -.
DR InParanoid; Q8CGM1; -.
DR OMA; GNILMPM; -.
DR OrthoDB; 4181250at2759; -.
DR PhylomeDB; Q8CGM1; -.
DR TreeFam; TF331634; -.
DR BioGRID-ORCS; 230775; 9 hits in 78 CRISPR screens.
DR ChiTaRS; Adgrb2; mouse.
DR PRO; PR:Q8CGM1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CGM1; Protein.
DR Bgee; ENSMUSG00000028782; Expressed in primary visual cortex and 135 other cell types or tissues.
DR ExpressionAtlas; Q8CGM1; baseline and differential.
DR Genevisible; Q8CGM1; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0033173; P:calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:InterPro.
DR GO; GO:0007422; P:peripheral nervous system development; IDA:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR CDD; cd15988; 7tmB2_BAI2; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 4.
DR InterPro; IPR043838; AGRB_N.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR008077; GPCR_2_brain_angio_inhib.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR10239:SF32; ADHESION G PROTEIN-COUPLED RECEPTOR B2; 1.
DR PANTHER; PTHR10239; ISTHMIN-2; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF19188; AGRB_N; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00090; TSP_1; 4.
DR PRINTS; PR01694; BAIPRECURSOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Proteoglycan; Receptor; Reference proteome; Repeat; Secreted; Signal;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1561
FT /note="Adhesion G protein-coupled receptor B2"
FT /id="PRO_0000245613"
FT TOPO_DOM 21..930
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 931..951
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 952..959
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 960..980
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 981..988
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 989..1009
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1010..1030
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1031..1051
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1052..1072
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1073..1093
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1094..1115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1116..1136
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1137..1147
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1148..1168
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1169..1561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 300..353
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 355..408
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 410..463
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 466..519
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 865..917
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 757..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 287..288
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250|UniProtKB:O60241"
FT MOD_RES 1345
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:O60241"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 861
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 312..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 316..352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 327..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 367..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 371..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 382..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 422..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 426..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 437..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 478..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 482..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 493..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 525..560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 548..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 868..900
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 888..902
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT VAR_SEQ 299..353
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019762"
FT VAR_SEQ 1113..1145
FT /note="SERCPWASLLLPCSACGAVPSPLLSSASARNAM -> RLSWNLWGYGSQLCL
FT FPKLPR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019763"
FT CONFLICT 116
FT /note="P -> L (in Ref. 1; AAN86965)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="Missing (in Ref. 1; AAN86965)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="Q -> K (in Ref. 1; AAN86965)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="R -> G (in Ref. 2; BAE34635)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="D -> G (in Ref. 2; BAE34635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1179
FT /note="A -> V (in Ref. 2; BAE34635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1316
FT /note="N -> D (in Ref. 2; BAE25937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1467
FT /note="Missing (in Ref. 2; BAE25937/BAE25805)"
FT /evidence="ECO:0000305"
FT CONFLICT 1550
FT /note="T -> P (in Ref. 1; AAN86965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1561 AA; 169863 MW; 3B3EB731F619CBA3 CRC64;
MTPACPLLLS VILSLRLATA FDPAPSACSA LASGVLYGAF SLQDLFPTIA SGCSWTLENP
DPTKYSLYLR FNRQEQVCTH FAPRLLPLDH YLVNFTCLRP GPEEATARAE SEVGRPEEEE
EEAAAAASGL ELCGGSGPFT FLHFDKNFVQ LCLSAEPSEA PRLLAPAALA FRFVEVLLIN
NNNSSQFTCG VLCRWSEECG RAAGRACGFA QPGCSCPGEA GANPATTTSP GPPVAHTLSN
ALVPGGPAPP AEADLHSGSS NDLFTTEMRY GEEPEEEPKV KTQWPRSADE PGLYMAQTGD
PAAEEWSPWS VCSLTCGQGL QVRTRSCVSS PYGTLCSGPL RETRPCNNSA TCPVHGVWEE
WGSWSLCSRS CGRGSRSRMR TCVPPQHGGK ACEGPELQTK LCSMAACPVE GQWLEWGPWG
PCSSSCANGT QQRSRKCSVA GPAWATCAGA LTDTRECSNL DCPATDGKWG PWNAWSLCSK
TCDTGWQRRF RMCQASGTQG YPCEGTGEEV KPCSEKRCPA FHEMCRDEYV MLMTWKRAAA
GEIIYNKCPP NASGSASRRC LLSAQGVAYW GLPSFARCIS HEYRYLYLSL REHLAKGQRM
LAGEGMSQVV RSLQELLARR TYYSGDLLFS VDILRNVTDT FKRATYVPSA DDVQRFFQVV
SFMVDSENKD KWDDAQQVSP GSVHLLRVVE DFIHLVGDAL KAFQSSLIVT DNLVISIQRE
PISAVSSDIT FPMRGRRGMK DWVRHSEDRL FLPKEVLSLS SPGKPATPGA ATAGSPGRGR
GPGTVPPGPG HAHQRLLPAD PEESSSYFVI GAVLYRTLGL ILPPPRPPLA VTSRVMTVTV
RPPTQPPAEP LITVELSYII NGTTDPHCAS WDYSRADTNS GDWNTESCQT LETQAAHTRC
QCQHLSTFAV LAQPPKDLTL ELAGAPSVPL VIGCAVSCMA LLTLLAIYAA FWRFIKSERS
IILLNFCLSI LASNILILVG QSRVLSKGVC TMTAAFLHFF FLSSFCWVLT EAWQSYLAVI
GRMRTRLVRK RFLCLGWGLP ALVVAVSVGF TRTKGYGTSS YCWLSLEGGL LYAFVGPAAV
IVLVNMLIGI IVFNKLMARD GVSDKSKKQR AGSERCPWAS LLLPCSACGA VPSPLLSSAS
ARNAMASLWS SCVVLPLLAL TWMSAVLAMT DRRSVLFQAL FAVFNSAQGF VITAVHCFLR
REVQDVVKCQ MGVCRADESE DSPDSCKNGQ LQILSDFEKD VDLACQTVLF KEVNTCNPST
ITGTLSRLSL DEDEEPKSCL VGPEGGLSFS PLPGNILVPM AASPGLGEPP PPQETNPVYM
CGEGGLRQLD LTWIRQSEPG SEGDYMVLPR RTLSLQPGGG GTAGEEAPRA RPEGTPRRAA
KTVAHTEGYP SFLSVEHSGL GLGPAYGSLQ NPYGMTFQPP PPTPSARQVP EPGERSRTMP
RTVPGSTMKL GSLERKKLRY SDLDFEKVMH TRKRHSELYH ELNQKFHTFD RYRSQSSAKE
KPSPPGGRPG LSQHRRHQSW STFKSMTLGS LPPKPRERLA LHRTAAWEPT EPPDGDFQTE
V
//
