ID   AGRF5_RAT               Reviewed;        1349 AA.
AC   Q9WVT0;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=Adhesion G protein-coupled receptor F5;
DE   AltName: Full=G protein-coupled hepta-helical receptor Ig-hepta;
DE            Short=Ig-Hepta {ECO:0000303|PubMed:10391944, ECO:0000303|PubMed:11973329};
DE   AltName: Full=G protein-coupled receptor 116;
DE   Flags: Precursor;
GN   Name=Adgrf5; Synonyms=Gpr116, Gprhep;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR
RP   LOCATION, GLYCOSYLATION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Lung;
RX   PubMed=10391944; DOI=10.1074/jbc.274.28.19957;
RA   Abe J., Suzuki H., Notoya M., Yamamoto T., Hirose S.;
RT   "Ig-hepta, a novel member of the G protein-coupled hepta-helical receptor
RT   (GPCR) family that has immunoglobulin-like repeats in a long N-terminal
RT   extracellular domain and defines a new subfamily of GPCRs.";
RL   J. Biol. Chem. 274:19957-19964(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 224-233 AND 994-1003, MUTAGENESIS OF THR-994,
RP   PROTEOLYTIC PROCESSING, AND GLYCOSYLATION.
RX   PubMed=11973329; DOI=10.1074/jbc.m110877200;
RA   Abe J., Fukuzawa T., Hirose S.;
RT   "Cleavage of Ig-Hepta at a 'SEA' module and at a conserved G protein-
RT   coupled receptor proteolytic site.";
RL   J. Biol. Chem. 277:23391-23398(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 52-60, PROTEOLYTIC PROCESSING, CLEAVAGE BY FURIN,
RP   GLYCOSYLATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=16882675; DOI=10.1093/jb/mvj170;
RA   Fukuzawa T., Hirose S.;
RT   "Multiple processing of Ig-Hepta/GPR116, a G protein-coupled receptor with
RT   immunoglobulin (Ig)-like repeats, and generation of EGF2-like fragment.";
RL   J. Biochem. 140:445-452(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [5]
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   [6]
RP   IDENTIFICATION OF THE TETHERED AGONIST.
RX   PubMed=36073784; DOI=10.7554/elife.69061;
RA   Bridges J.P., Safina C., Pirard B., Brown K., Filuta A., Panchanathan R.,
RA   Bouhelal R., Reymann N., Patel S., Seuwen K., Miller W.E., Ludwig M.G.;
RT   "Regulation of pulmonary surfactant by the adhesion GPCR GPR116/ADGRF5
RT   requires a tethered agonist-mediated activation mechanism.";
RL   Elife 11:0-0(2022).
CC   -!- FUNCTION: Receptor that plays a critical role in lung surfactant
CC       homeostasis. May play a role in controlling adipocyte function.
CC       {ECO:0000250|UniProtKB:G5E8Q8}.
CC   -!- FUNCTION: Adhesion G protein-coupled receptor. In alveolar type II
CC       (ATII or AT2) cells, required for normal lung surfactant homeostasis.
CC       Modulation of both surfactant secretion and uptake by ATII cells is
CC       mediated by the downstream activation of GNAQ/GNA11 proteins and may be
CC       a consequence of increased cortical F-actin assembly induced by ADGRF5
CC       activation. In the kidney, may play a role in the regulation of acid
CC       excretion into the primary urine, possibly by regulating the surface
CC       expression of V-ATPase proton pump. As a receptor for soluble FNDC4
CC       (sFNDC4), required for proper systemic glucose tolerance, specifically
CC       sensitizing white adipose tissue to insulin. Also plays a role in
CC       sFNDC4-induced decrease of local inflammation in white adipose tissue.
CC       {ECO:0000250|UniProtKB:G5E8Q8}.
CC   -!- ACTIVITY REGULATION: As an adhesion G protein-coupled receptor (aGPCR)
CC       exhibits a large N-terminal extracellular domain containing highly
CC       conserved GPCR autoproteolysis-inducing (GAIN) domain. During
CC       synthesis, intracellular autoproteolytic processing of nascent chain
CC       within the GAIN domain generates a mature protein, consisting of an N-
CC       terminal fragment that is non-covalently linked to the C-terminal
CC       fragment. The mature protein is routed to the plasma membrane where the
CC       N- and C-terminal fragments remain associated, forming the
CC       holoreceptor. Dissociation of the aGPCR fragments stimulates G protein
CC       signaling through the action of the tethered-peptide agonist stalk that
CC       is occluded within the GAIN domain in the holoreceptor form. This
CC       dissociation might be induced by ligand binding, such as that of
CC       sFNDC4. {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:10391944). Heterodimer of
CC       2 chains generated by proteolytic processing; the large extracellular
CC       N-terminal fragment and the membrane-bound C-terminal fragment
CC       predominantly remain associated and non-covalently linked
CC       (PubMed:11973329). Fragment generates by the processing enzyme furin
CC       remains attached to the extracellular N-terminal fragment
CC       (PubMed:16882675). Interacts (via N-terminal extracellular domain) with
CC       SFTPD (By similarity). {ECO:0000250|UniProtKB:G5E8Q8,
CC       ECO:0000269|PubMed:10391944, ECO:0000269|PubMed:11973329,
CC       ECO:0000269|PubMed:16882675}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10391944,
CC       ECO:0000269|PubMed:16882675}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the lung and to a much lesser
CC       extent in the kidney and heart. Dense localization in alveolar walls of
CC       the lung and in the intercalated cells of the collecting duct of the
CC       kidney. {ECO:0000269|PubMed:10391944}.
CC   -!- DEVELOPMENTAL STAGE: In the lung, expression increases from postnatal
CC       day 3 to 14 weeks of age. {ECO:0000269|PubMed:10391944}.
CC   -!- PTM: Highly glycosylated. {ECO:0000269|PubMed:10391944,
CC       ECO:0000269|PubMed:11973329, ECO:0000269|PubMed:16882675}.
CC   -!- PTM: Proteolytically cleaved at multiple sites: one in the GPS region
CC       of the GAIN-B domain (S1 site) and the other in the SEA domain (S2
CC       site). The proteolytic cleavage at S1 site generates an extracellular
CC       subunit and a seven-transmembrane subunit. The proteolytic cleavage at
CC       S2 site generates a fragment that undergoes proteolytic cleavage by the
CC       processing enzyme furin. {ECO:0000269|PubMed:11973329,
CC       ECO:0000269|PubMed:16882675}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 2 family.
CC       Adhesion G protein-coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB019120; BAA82518.1; -; mRNA.
DR   RefSeq; NP_620810.1; NM_139110.2.
DR   AlphaFoldDB; Q9WVT0; -.
DR   SMR; Q9WVT0; -.
DR   FunCoup; Q9WVT0; 69.
DR   STRING; 10116.ENSRNOP00000071238; -.
DR   MEROPS; P02.032; -.
DR   GlyCosmos; Q9WVT0; 20 sites, No reported glycans.
DR   GlyGen; Q9WVT0; 21 sites.
DR   iPTMnet; Q9WVT0; -.
DR   PhosphoSitePlus; Q9WVT0; -.
DR   PaxDb; 10116-ENSRNOP00000071238; -.
DR   Ensembl; ENSRNOT00000015223.4; ENSRNOP00000015223.1; ENSRNOG00000011154.8.
DR   Ensembl; ENSRNOT00055034326; ENSRNOP00055027807; ENSRNOG00055020095.
DR   Ensembl; ENSRNOT00060037919; ENSRNOP00060031267; ENSRNOG00060021816.
DR   Ensembl; ENSRNOT00065039830; ENSRNOP00065032401; ENSRNOG00065023255.
DR   GeneID; 245977; -.
DR   KEGG; rno:245977; -.
DR   UCSC; RGD:621679; rat.
DR   AGR; RGD:621679; -.
DR   CTD; 221395; -.
DR   RGD; 621679; Adgrf5.
DR   eggNOG; KOG4193; Eukaryota.
DR   GeneTree; ENSGT00940000154603; -.
DR   HOGENOM; CLU_002753_3_5_1; -.
DR   InParanoid; Q9WVT0; -.
DR   PhylomeDB; Q9WVT0; -.
DR   Reactome; R-RNO-5683826; Surfactant metabolism.
DR   PRO; PR:Q9WVT0; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000011154; Expressed in lung and 19 other cell types or tissues.
DR   ExpressionAtlas; Q9WVT0; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; EXP:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0006112; P:energy reserve metabolic process; ISO:RGD.
DR   GO; GO:0048821; P:erythrocyte development; ISO:RGD.
DR   GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR   GO; GO:0003094; P:glomerular filtration; ISO:RGD.
DR   GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR   GO; GO:0043031; P:negative regulation of macrophage activation; ISO:RGD.
DR   GO; GO:0061626; P:pharyngeal arch artery morphogenesis; ISO:RGD.
DR   GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; ISO:RGD.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; ISO:RGD.
DR   GO; GO:0043129; P:surfactant homeostasis; ISO:RGD.
DR   FunFam; 1.20.1070.10:FF:000058; Adhesion G protein-coupled receptor F5; 1.
DR   FunFam; 2.60.40.10:FF:002239; Adhesion G protein-coupled receptor F5; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   Gene3D; 3.30.70.960; SEA domain; 1.
DR   InterPro; IPR057400; ADGRF3/5_N.
DR   InterPro; IPR051587; Adhesion_GPCR.
DR   InterPro; IPR057244; GAIN_B.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR008078; GPCR_2_Ig-hepta-like_rcpt.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin_dom.
DR   InterPro; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   PANTHER; PTHR45813:SF4; ADHESION G PROTEIN-COUPLED RECEPTOR F5; 1.
DR   PANTHER; PTHR45813; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF25387; ADGRF3_N; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF01390; SEA; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PRINTS; PR01695; IGHEPTARCPTR.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF82671; SEA domain; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GAIN_B; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS50024; SEA; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond;
KW   G protein-coupled receptor; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1349
FT                   /note="Adhesion G protein-coupled receptor F5"
FT                   /id="PRO_0000012897"
FT   TOPO_DOM        25..1016
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1017..1036
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1037..1055
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1056..1078
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1079..1097
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1098..1120
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1121..1131
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1132..1154
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1155..1173
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1174..1196
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1197..1216
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1217..1239
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1240..1248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        1249..1271
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1272..1349
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          163..271
FT                   /note="SEA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT   DOMAIN          268..366
FT                   /note="Ig-like 1"
FT   DOMAIN          367..464
FT                   /note="Ig-like 2"
FT   DOMAIN          469..559
FT                   /note="Ig-like 3"
FT   DOMAIN          842..1006
FT                   /note="GAIN-B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          954..1006
FT                   /note="GPS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   REGION          994..1009
FT                   /note="Tethered agonist"
FT                   /evidence="ECO:0000305|PubMed:36073784"
FT   REGION          1329..1349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1329..1343
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            51..52
FT                   /note="Cleavage; by furin"
FT                   /evidence="ECO:0000269|PubMed:16882675"
FT   SITE            223..224
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000269|PubMed:11973329"
FT   SITE            993..994
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098,
FT                   ECO:0000269|PubMed:11973329"
FT   MOD_RES         819
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16641100"
FT   MOD_RES         1303
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:G5E8Q8"
FT   MOD_RES         1310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:G5E8Q8"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        254
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        470
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        538
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        649
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        666
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        820
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        958
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        963
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1085
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        291..348
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        389..447
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        490..543
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        954..988
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   DISULFID        973..990
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT   MUTAGEN         994
FT                   /note="T->A: Abolishes cleavage."
FT                   /evidence="ECO:0000269|PubMed:11973329"
SQ   SEQUENCE   1349 AA;  149446 MW;  104CF1D9A35B1409 CRC64;
     MKSSRTVTLY FVLIVICSSE ATWSRPAEPI VHPLILQEHE LAGEELLRPK RAVAVGGPVA
     EEYTVDVEIS FENVSFLESI RAHLNSLRFP VQGNGTDILS MAMTTVCTPT GNDLLCFCEK
     GYQWPEERCL SSLTCQEHDS ALPGRYCNCL KGLPPQGPFC QLPETYITLK IKVRLNIGFQ
     EDLENTSSAL YRSYKTDLER AFRAGYRTLP GFRSVTVTQF TKGSVVVDYI VEVASAPLPG
     SIHKANEQVI QNLNQTYKMD YNSFQGTPSN ETKFTVTPEF IFEGDNVTLE CESEFVSSNT
     SWFYGEKRSD IQNSDKFSIH TSIINNISLV TRLTIFNFTQ HDAGLYGCNV TLDIFEYGTV
     RKLDVTPIRI LAKEERKVVC DNNPISLNCC SENIANWSRI EWKQEGKINI EGTPETDLES
     SCSTYTLKAD GTQCPSGSSG TTVIYTCEFV SVYGAKGSKN IAVTFTSVAN LTITPDPISV
     SEGQSFSITC LSDVSSFDEV YWNTSAGIKI HPRFYTMRRY RDGAESVLTV KTSTREWNGT
     YHCIFRYKNS YSIATKDVTV HPLPLESDIM MDPLEASGLC TSSHQFKCCI EENDGEEYIV
     TFHVDSSSFP AEREVIGKQA CYTYSLPGKL PSRCPKDIDV FCHFTNAANS SVRSPSMKLT
     LVPGKNITCQ DPIIGIGEPG KVIQKLCQFA GVSRSPGQTI GGTVTYKCVG SQWKEETRAC
     ISAPINGLLQ LAKALIKSPS QDQKLPKYLR DLSVSTGKEE QDIRSSPGSL GAIISILDLL
     STVPTQVNSE MMRDILATIN VILDKSTLNS WEKLLQQQSN QSSQFLQSVE RFSKALELGD
     STPPFLFHPN VQMKSMVIKR GHAQMYQQKF VFTDSDLWGD VAIDECQLGS LQPDSSIVTV
     AFPTLKAILA QDGQRKTPSN SLVMTTTVSH NIVKPFRISM TFKNNHRSGG KPQCVFWNFS
     LANNTGGWDS SGCTVEDDGR DNRDRVFCKC NHLTSFSILM SPDSPDPGSL LKILLDIISY
     IGLGFSIVSL AACLVVEAMV WKSVTKNRTS YMRHICIVNI ALCLLIADIW FIVAGAIHDG
     HYPLNETACV AATFFIHFFY LSVFFWMLTL GLMLFYRLIF ILHDASKSTQ KAIAFSLGYG
     CPLIISSITV GVTQPQEVYM RKNACWLNWE DTRALLAFAI PALIIVVVNV SITVVVITKI
     LRPSVGDKPG KQEKSSLFQI SKSIGVLTPL LGLTWGFGLA TVIQGSNAVF HIIFTLLNAF
     QGLFILLFGC LWDQKVQEAL LHKFSLSRWS SQHSKSTSLG SSTPVFSMSS PISRRFNNLF
     GKTGTYNVST PETTSSSVEN SSSAYSLLN
//