AGRB1_RAT
ID AGRB1_RAT Reviewed; 1577 AA.
AC C0HL12;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Adhesion G protein-coupled receptor B1 {ECO:0000312|RGD:1305608};
DE AltName: Full=Brain-specific angiogenesis inhibitor 1 {ECO:0000312|RGD:1305608};
DE Contains:
DE RecName: Full=Vasculostatin-120 {ECO:0000250|UniProtKB:O14514};
DE Short=Vstat120 {ECO:0000250|UniProtKB:O14514};
DE Contains:
DE RecName: Full=Vasculostatin-40 {ECO:0000250|UniProtKB:O14514};
DE Short=Vstat-40 {ECO:0000250|UniProtKB:O14514};
DE Flags: Precursor;
GN Name=Adgrb1 {ECO:0000312|RGD:1305608};
GN Synonyms=Bai1 {ECO:0000312|RGD:1305608};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000303|PubMed:15057822};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PARD3 AND TIAM1, AND SUBCELLULAR LOCATION.
RX PubMed=23595754; DOI=10.1523/jneurosci.3978-12.2013;
RA Duman J.G., Tzeng C.P., Tu Y.K., Munjal T., Schwechter B., Ho T.S.,
RA Tolias K.F.;
RT "The adhesion-GPCR BAI1 regulates synaptogenesis by controlling the
RT recruitment of the Par3/Tiam1 polarity complex to synaptic sites.";
RL J. Neurosci. 33:6964-6978(2013).
CC -!- FUNCTION: Phosphatidylserine receptor which enhances the engulfment of
CC apoptotic cells (By similarity). Also mediates the binding and
CC engulfment of Gram-negative bacteria (By similarity). Stimulates
CC production of reactive oxygen species by macrophages in response to
CC Gram-negative bacteria, resulting in enhanced microbicidal macrophage
CC activity (By similarity). In the gastric mucosa, required for
CC recognition and engulfment of apoptotic gastric epithelial cells (By
CC similarity). Promotes myoblast fusion (By similarity). Activates the
CC Rho pathway in a G-protein-dependent manner (By similarity). Inhibits
CC MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting
CC DLG4 stability and regulating synaptic plasticity (By similarity).
CC Required for the formation of dendritic spines by ensuring the correct
CC dendritic localization of PARD3 and TIAM1 (PubMed:23595754). Potent
CC inhibitor of angiogenesis in brain and may play a significant role as a
CC mediator of the p53/TP53 signal in suppression of glioblastoma (By
CC similarity). {ECO:0000250|UniProtKB:O14514,
CC ECO:0000269|PubMed:23595754}.
CC -!- FUNCTION: [Vasculostatin-120]: Inhibits angiogenesis in a CD36-
CC dependent manner. {ECO:0000250|UniProtKB:O14514}.
CC -!- FUNCTION: [Vasculostatin-40]: Inhibits angiogenesis.
CC {ECO:0000250|UniProtKB:O14514}.
CC -!- SUBUNIT: Interacts with ELMO1 and DOCK1 (By similarity). When bound to
CC ELMO1 and DOCK1, acts as a module to promote apoptotic cell engulfment
CC (By similarity). Interacts with MDM2; the interaction results in
CC inhibition of MDM2-mediated ubiquitination and degradation of
CC DLG4/PSD95 (By similarity). Interacts with PARD3 and TIAM1; the
CC interaction is required for correct dendritic localization of PARD3 and
CC TIAM1 and for dendritic spine formation (PubMed:23595754). Interacts
CC with MAGI1, MAGI3 and BAIAP2 (By similarity). Interacts with PHYHIP (By
CC similarity). Interacts with DLG4 (via PDZ domain) (By similarity).
CC Vasculostatin-120: Interacts with CD36 (By similarity). Vasculostatin-
CC 120: Interacts with ARRB2 (By similarity). Interacts with BAIAP3; this
CC interaction is direct (By similarity). {ECO:0000250|UniProtKB:O14514,
CC ECO:0000250|UniProtKB:Q3UHD1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14514};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, phagocytic
CC cup {ECO:0000250|UniProtKB:Q3UHD1}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q3UHD1}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:23595754}. Postsynaptic density
CC {ECO:0000269|PubMed:23595754}.
CC -!- SUBCELLULAR LOCATION: [Vasculostatin-120]: Secreted
CC {ECO:0000250|UniProtKB:O14514}.
CC -!- SUBCELLULAR LOCATION: [Vasculostatin-40]: Secreted
CC {ECO:0000250|UniProtKB:O14514}.
CC -!- DOMAIN: The TSP type-1 repeats in the extracellular domain mediate
CC binding to phosphatidylserine. They are also required for bacterial
CC recognition and binding to bacterial outer membrane lipopolysaccharide.
CC {ECO:0000250|UniProtKB:Q3UHD1}.
CC -!- PTM: Proteolytically cleaved to produce vasculostatin-40 and
CC vasculostatin-120. Vasculostatin-40 is the major form and is produced
CC through proteolytic cleavage by MMP14 between residues 317 and 325 with
CC cleavage likely to be between Ser-322 and Leu-323.
CC {ECO:0000250|UniProtKB:O14514}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:O14514}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; AABR07058422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001164068.2; NM_001170597.2.
DR AlphaFoldDB; C0HL12; -.
DR SMR; C0HL12; -.
DR GlyGen; C0HL12; 1 site.
DR GeneID; 362931; -.
DR KEGG; rno:362931; -.
DR CTD; 575; -.
DR RGD; 1305608; Adgrb1.
DR OrthoDB; 27621at2759; -.
DR PRO; PR:C0HL12; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0001891; C:phagocytic cup; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0043277; P:apoptotic cell clearance; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD.
DR GO; GO:0043652; P:engulfment of apoptotic cell; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR GO; GO:0006910; P:phagocytosis, recognition; ISO:RGD.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; ISO:RGD.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:RGD.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0051963; P:regulation of synapse assembly; IDA:SynGO.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR Gene3D; 2.20.100.10; -; 5.
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; PF02793; HRM; 1.
DR Pfam; PF00090; TSP_1; 5.
DR PRINTS; PR01694; BAIPRECURSOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF82895; SSF82895; 5.
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; 5.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Immunity; Innate immunity;
KW Membrane; Myogenesis; Neurogenesis; Phagocytosis; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Secreted; Signal; Synapse; Transducer;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1577
FT /note="Adhesion G protein-coupled receptor B1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441808"
FT CHAIN 34..923
FT /note="Vasculostatin-120"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT /id="PRO_0000441810"
FT CHAIN 34..?323
FT /note="Vasculostatin-40"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT /id="PRO_0000441809"
FT TOPO_DOM 34..944
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 945..965
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 966..976
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 977..997
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 998..1004
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1005..1025
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1026..1048
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1049..1069
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1070..1089
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1090..1110
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1111..1132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1133..1153
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1154..1162
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1163..1183
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1184..1577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 257..311
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 350..403
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 405..458
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 463..516
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 518..571
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 877..934
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 310..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..943
FT /note="N-terminal stalk following vasculostatin-120
FT cleavage which is not required for signaling activity"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT REGION 1359..1577
FT /note="Involved in interaction with MAGI1"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT REGION 1378..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1577
FT /note="Indispensable for interaction with MAGI1"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT COMPBIAS 1385..1429
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 922..923
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT MOD_RES 605
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14514"
FT MOD_RES 1462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHD1"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 269..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 273..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 284..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 362..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 366..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 377..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 417..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 421..457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 432..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 475..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 479..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 490..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 530..565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 534..570
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 545..555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
SQ SEQUENCE 1577 AA; 172883 MW; 0DB6FCC202F80EEA CRC64;
MRGQAAAPGP IWILAPLLLL LLLLGRWARA ASGADIGPGT EQCTTLVQGK FFGYFSAAAV
FPANASRCSW TLRNPDPRRY TLYMKVAKAP APCSGPGRVR TYQFDSFLES TRTYLGVESF
DEVLRLCDPS APLAFLQASK QFLQMQRQQP PQDGDLGPQG SGDDFSVEYL VVGNRNPSHA
ACQMLCRWLD ACLAGSRSSH PCGIMQTPCA CLGGEAGDTA SSPLVPRGDV CLRDGVAGGP
ENCLTSLTQD RGGHGSAGGW KLWSLWGECT RDCGGGLQTR TRTCSPTLGV EGRGCEGVLE
EGRLCNRKAC GPTGRTSSRS QSLRSTDARR REEFGDELQQ FGFPSPQTGD PAAEEWSPWS
VCSSTCGEGW QTRTRFCVSS SYSTQCSGPL REQRLCNNSA VCPVHGAWDE WSPWSLCSST
CGRGFRDRTR TCRPPQFGGN PCEGPEKQTK FCNIALCPGR AVDGNWNEWS SWSTCSASCS
QGRQQRTREC NGPSYGGAEC QGHWVETRDC FLQQCPVDGK WQAWASWGSC SVTCGGGSQR
RERVCSGPFF GGAACQGPQD EYRQCGAQRC PEPHEICDED NFGAVVWKET PAGEVAAVRC
PRNATGLILR RCELDEEGIA FWEPPTYIRC VSIDYRNIQM MTREHLAKAQ RGLPGEGVSE
VIQTLLEISQ DGTSYSGDLL STIDVLRNMT EIFRRAYYSP TPGDVQNFVQ IISNLLAEEN
RDKWEEAQLM GPNAKELFRL VEDFVDVIGF RMKDLRDAYQ VTDNLVLSIH KLPASGATDI
SFPMKGWRAT GDWAKVPEDR VTVSKSVFST GLAEADDSSV FVVGTVLYRN LGSFLALQRN
TTVLNSKVIS VTVKPPPRSL LTPLEIEFAH MYNGTTNQTC ILWDETDGPS SSAPPQLGPW
SWRGCRTVPL DALRTRCLCD RLSTFAILAQ LSADATMDKV TVPSVTLIVG CGVSSLTLLM
LVIIYVSVWR YIRSERSVIL INFCLSIISS NALILIGQTQ TRNKVVCTLV AAFLHFFFLS
SFCWVLTEAW QSYMAVTGRL RSRLVRKRFL CLGWGLPALV VAISVGFTKA KGYSTMNYCW
LSLEGGLLYA FVGPAAAVVL VNMVIGILVF NKLVSKDGIT DKKLKERAGA SLWSSCVVLP
LLALTWMSAV LAVTDRRSAL FQILFAVFDS LEGFVIVMVH CILRREVQDA VKCRVVDRQE
EGNGDSGGSF QNGHAQLMTD FEKDVDLACR SVLNKDIAAC RTATITGTFK RPSLPEEEKM
KLAKGPPPTF NSLPANVSKL HLHGSPRYPG GPLPDFPNHS LTLKKDKAPK SSFIGDGDIF
KKLDSELSRA QEKALDTSYV ILPTATATLR PKPKEEPKYS INIDQMPQTR LIHLSMAPDA
SFPTRSPPAR EPPGGAPPEV PPVQPPPPPP PPPPPQQPIP PPPSLEPAPP SLGDTGEPSA
HPGPSSGAGT KNENVATLSV SSLERRKSRY AELDFEKIMH TRKRHQDMFQ DLNRKLQHAA
EKEKEVPGVD NKPEKQQTPN KRAWESLRKP HGTPAWVKKE LEPLPPSPLE LRSVEWEKAG
ATIPLVGQDI IDLQTEV
