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AGRB2_MOUSE
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   03-AUG-2022, entry version 138.
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}.
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: Proteolytic processes at the GPS domain; this cleavage modulates
CC       receptor activity. Additionally, furin is involved in the cleavage at
CC       another site, in the middle of the extracellular domain, generating a
CC       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; 6.
DR   IntAct; Q8CGM1; 5.
DR   MINT; Q8CGM1; -.
DR   STRING; 10090.ENSMUSP00000101638; -.
DR   MEROPS; P02.029; -.
DR   GlyConnect; 2108; 8 N-Linked glycans (2 sites).
DR   GlyGen; Q8CGM1; 8 sites, 8 N-linked glycans (2 sites).
DR   iPTMnet; Q8CGM1; -.
DR   PhosphoSitePlus; Q8CGM1; -.
DR   MaxQB; Q8CGM1; -.
DR   PaxDb; Q8CGM1; -.
DR   PRIDE; Q8CGM1; -.
DR   ProteomicsDB; 296126; -. [Q8CGM1-1]
DR   ProteomicsDB; 296127; -. [Q8CGM1-2]
DR   ProteomicsDB; 296128; -. [Q8CGM1-3]
DR   Antibodypedia; 16794; 300 antibodies from 33 providers.
DR   DNASU; 230775; -.
DR   Ensembl; ENSMUST00000106015; ENSMUSP00000101636; ENSMUSG00000028782. [Q8CGM1-1]
DR   Ensembl; ENSMUST00000106017; ENSMUSP00000101638; ENSMUSG00000028782. [Q8CGM1-3]
DR   Ensembl; ENSMUST00000121049; ENSMUSP00000112869; ENSMUSG00000028782. [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   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; NILMPMA; -.
DR   OrthoDB; 27621at2759; -.
DR   PhylomeDB; Q8CGM1; -.
DR   TreeFam; TF331634; -.
DR   BioGRID-ORCS; 230775; 8 hits in 73 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 133 other tissues.
DR   ExpressionAtlas; Q8CGM1; baseline and differential.
DR   Genevisible; Q8CGM1; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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   Gene3D; 2.20.100.10; -; 4.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 4.10.1240.10; -; 1.
DR   InterPro; IPR043838; AGRB_N.
DR   InterPro; IPR032471; GAIN_dom_N.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like.
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   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; SSF82895; SSF82895; 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   Receptor; Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW   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        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
 
 
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