AGRF5_HUMAN
ID AGRF5_HUMAN Reviewed; 1346 AA.
AC Q8IZF2; O94858; Q5TF06; Q6RGN2; Q86SP0; Q9Y3Z2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Adhesion G protein-coupled receptor F5 {ECO:0000303|PubMed:25713288};
DE AltName: Full=G-protein coupled receptor 116;
DE Flags: Precursor;
GN Name=ADGRF5 {ECO:0000312|HGNC:HGNC:19030}; Synonyms=GPR116, KIAA0758;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=12435584; DOI=10.1016/s0014-5793(02)03574-3;
RA Fredriksson R., Lagerstroem M.C., Hoeglund P.J., Schioeth H.B.;
RT "Novel human G protein-coupled receptors with long N-terminals containing
RT GPS domains and Ser/Thr-rich regions.";
RL FEBS Lett. 531:407-414(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-604.
RC TISSUE=Brain;
RA Bonner T.I., Nagle J.W., Kauffman D.;
RT "Complete coding sequence of GPR116.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS MET-604
RP AND THR-856.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-613 (ISOFORM 1), AND VARIANTS MET-604 AND ILE-801.
RC TISSUE=Brain, and Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS MET-604
RP AND THR-856.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 949-1062.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-256 AND ASN-315.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP NOMENCLATURE.
RX PubMed=25713288; DOI=10.1124/pr.114.009647;
RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT protein-coupled receptors.";
RL Pharmacol. Rev. 67:338-367(2015).
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 -!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer of 2 chains generated
CC by proteolytic processing; the large extracellular N-terminal fragment
CC and the membrane-bound C-terminal fragment predominantly remain
CC associated and non-covalently linked. Fragment generates by the
CC processing enzyme furin remains attached to the extracellular N-
CC terminal fragment. Interacts (via N-terminal extracellular domain) with
CC SFTPD. {ECO:0000250|UniProtKB:G5E8Q8, ECO:0000250|UniProtKB:Q9WVT0}.
CC -!- INTERACTION:
CC Q8IZF2; Q9NPB3: CABP2; NbExp=3; IntAct=EBI-7600130, EBI-12011224;
CC Q8IZF2; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-7600130, EBI-10242151;
CC Q8IZF2; Q13952-2: NFYC; NbExp=3; IntAct=EBI-7600130, EBI-11956831;
CC Q8IZF2; P55735-3: SEC13; NbExp=3; IntAct=EBI-7600130, EBI-12235008;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9WVT0};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IZF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZF2-2; Sequence=VSP_010837, VSP_010838;
CC Name=3;
CC IsoId=Q8IZF2-3; Sequence=VSP_039130;
CC -!- PTM: Proteolytically cleaved at multiple sites: one in the GPS domain
CC (S1 site) and the other in the SEA domain (S2 site). The proteolytic
CC cleavage at S1 site generates an extracellular subunit and a seven-
CC transmembrane subunit. The proteolytic cleavage at S2 site generates a
CC fragment that undergoes proteolytic cleavage by the processing enzyme
CC furin. {ECO:0000250|UniProtKB:Q9WVT0}.
CC -!- PTM: Highly glycosylated. {ECO:0000250|UniProtKB:Q9WVT0}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34478.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB43394.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY140958; AAN46672.1; -; mRNA.
DR EMBL; AY498875; AAS21061.1; -; mRNA.
DR EMBL; AB018301; BAA34478.2; ALT_INIT; mRNA.
DR EMBL; AL050295; CAB43394.1; ALT_SEQ; mRNA.
DR EMBL; AL832125; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL096772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC066121; AAH66121.1; -; mRNA.
DR EMBL; AY255552; AAO85064.1; -; mRNA.
DR CCDS; CCDS4919.1; -. [Q8IZF2-1]
DR PIR; T08685; T08685.
DR RefSeq; NP_001091988.1; NM_001098518.1. [Q8IZF2-1]
DR RefSeq; NP_056049.4; NM_015234.4. [Q8IZF2-1]
DR AlphaFoldDB; Q8IZF2; -.
DR BioGRID; 128719; 6.
DR IntAct; Q8IZF2; 7.
DR MINT; Q8IZF2; -.
DR STRING; 9606.ENSP00000283296; -.
DR ChEMBL; CHEMBL4523888; -.
DR MEROPS; P02.019; -.
DR GlyConnect; 1914; 28 N-Linked glycans (14 sites).
DR GlyGen; Q8IZF2; 27 sites, 29 N-linked glycans (14 sites), 5 O-linked glycans (1 site).
DR iPTMnet; Q8IZF2; -.
DR PhosphoSitePlus; Q8IZF2; -.
DR BioMuta; ADGRF5; -.
DR DMDM; 229462973; -.
DR jPOST; Q8IZF2; -.
DR MassIVE; Q8IZF2; -.
DR PaxDb; Q8IZF2; -.
DR PeptideAtlas; Q8IZF2; -.
DR PRIDE; Q8IZF2; -.
DR ProteomicsDB; 71338; -. [Q8IZF2-1]
DR ProteomicsDB; 71339; -. [Q8IZF2-2]
DR ProteomicsDB; 71340; -. [Q8IZF2-3]
DR Antibodypedia; 16896; 244 antibodies from 28 providers.
DR DNASU; 221395; -.
DR Ensembl; ENST00000265417.7; ENSP00000265417.6; ENSG00000069122.19. [Q8IZF2-1]
DR Ensembl; ENST00000283296.12; ENSP00000283296.7; ENSG00000069122.19. [Q8IZF2-1]
DR GeneID; 221395; -.
DR KEGG; hsa:221395; -.
DR MANE-Select; ENST00000283296.12; ENSP00000283296.7; NM_001098518.2; NP_001091988.1.
DR UCSC; uc003oyo.5; human. [Q8IZF2-1]
DR CTD; 221395; -.
DR DisGeNET; 221395; -.
DR GeneCards; ADGRF5; -.
DR HGNC; HGNC:19030; ADGRF5.
DR HPA; ENSG00000069122; Tissue enhanced (lung).
DR neXtProt; NX_Q8IZF2; -.
DR OpenTargets; ENSG00000069122; -.
DR PharmGKB; PA134886165; -.
DR VEuPathDB; HostDB:ENSG00000069122; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000154603; -.
DR HOGENOM; CLU_002753_3_5_1; -.
DR InParanoid; Q8IZF2; -.
DR OMA; VADTWFI; -.
DR OrthoDB; 611778at2759; -.
DR PhylomeDB; Q8IZF2; -.
DR TreeFam; TF316380; -.
DR PathwayCommons; Q8IZF2; -.
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR SignaLink; Q8IZF2; -.
DR BioGRID-ORCS; 221395; 14 hits in 1070 CRISPR screens.
DR ChiTaRS; ADGRF5; human.
DR GeneWiki; GPR116; -.
DR GenomeRNAi; 221395; -.
DR Pharos; Q8IZF2; Tbio.
DR PRO; PR:Q8IZF2; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8IZF2; protein.
DR Bgee; ENSG00000069122; Expressed in lower lobe of lung and 194 other tissues.
DR Genevisible; Q8IZF2; HS.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IEA:Ensembl.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.30.70.960; -; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
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; IPR000082; SEA_dom.
DR InterPro; IPR036364; SEA_dom_sf.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 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; SSF48726; SSF48726; 2.
DR SUPFAM; SSF82671; SSF82671; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50024; SEA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1346
FT /note="Adhesion G protein-coupled receptor F5"
FT /id="PRO_0000012896"
FT TOPO_DOM 22..1006
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1007..1027
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1028..1053
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1054..1074
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1075..1090
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1091..1111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1112..1128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1129..1149
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1150..1173
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1174..1194
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1195..1220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1221..1241
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1242..1244
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1245..1265
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1266..1346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 166..273
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 267..368
FT /note="Ig-like 1"
FT DOMAIN 369..466
FT /note="Ig-like 2"
FT DOMAIN 471..561
FT /note="Ig-like 3"
FT DOMAIN 951..1002
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 1327..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 51..52
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250|UniProtKB:Q9WVT0"
FT SITE 226..227
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q9WVT0"
FT SITE 990..991
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:Q9WVT0"
FT MOD_RES 1300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:G5E8Q8"
FT MOD_RES 1307
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 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
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 931
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 982
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 293..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 391..449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 492..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 272..414
FT /note="NESNFFVTPEIIFEGDTVSLVCEKEVLSSNVSWRYEEQQLEIQNSSRFSIYT
FT ALFNNMTSVSKLTIHNITPGDAGEYVCKLILDIFEYECKKKIDVMPIQILANEEMKVMC
FT DNNPVSLNCCSQGNVNWSKVEWKQEGKINIPG -> R (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039130"
FT VAR_SEQ 1273..1292
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12435584"
FT /id="VSP_010837"
FT VAR_SEQ 1322..1346
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12435584"
FT /id="VSP_010838"
FT VARIANT 604
FT /note="T -> M (in dbSNP:rs586024)"
FT /evidence="ECO:0000269|PubMed:10048485,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.2"
FT /id="VAR_025326"
FT VARIANT 801
FT /note="V -> I (in dbSNP:rs9395218)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_055291"
FT VARIANT 856
FT /note="M -> T (in dbSNP:rs547499)"
FT /evidence="ECO:0000269|PubMed:10048485,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_024477"
FT CONFLICT 272
FT /note="Missing (in Ref. 1; AAN46672)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="V -> I (in Ref. 7; CAB43394)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="Q -> R (in Ref. 5; AL832125)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1346 AA; 149457 MW; 72A9D02B08218A60 CRC64;
MKSPRRTTLC LMFIVIYSSK AALNWNYEST IHPLSLHEHE PAGEEALRQK RAVATKSPTA
EEYTVNIEIS FENASFLDPI KAYLNSLSFP IHGNNTDQIT DILSINVTTV CRPAGNEIWC
SCETGYGWPR ERCLHNLICQ ERDVFLPGHH CSCLKELPPN GPFCLLQEDV TLNMRVRLNV
GFQEDLMNTS SALYRSYKTD LETAFRKGYG ILPGFKGVTV TGFKSGSVVV TYEVKTTPPS
LELIHKANEQ VVQSLNQTYK MDYNSFQAVT INESNFFVTP EIIFEGDTVS LVCEKEVLSS
NVSWRYEEQQ LEIQNSSRFS IYTALFNNMT SVSKLTIHNI TPGDAGEYVC KLILDIFEYE
CKKKIDVMPI QILANEEMKV MCDNNPVSLN CCSQGNVNWS KVEWKQEGKI NIPGTPETDI
DSSCSRYTLK ADGTQCPSGS SGTTVIYTCE FISAYGARGS ANIKVTFISV ANLTITPDPI
SVSEGQNFSI KCISDVSNYD EVYWNTSAGI KIYQRFYTTR RYLDGAESVL TVKTSTREWN
GTYHCIFRYK NSYSIATKDV IVHPLPLKLN IMVDPLEATV SCSGSHHIKC CIEEDGDYKV
TFHTGSSSLP AAKEVNKKQV CYKHNFNASS VSWCSKTVDV CCHFTNAANN SVWSPSMKLN
LVPGENITCQ DPVIGVGEPG KVIQKLCRFS NVPSSPESPI GGTITYKCVG SQWEEKRNDC
ISAPINSLLQ MAKALIKSPS QDEMLPTYLK DLSISIDKAE HEISSSPGSL GAIINILDLL
STVPTQVNSE MMTHVLSTVN VILGKPVLNT WKVLQQQWTN QSSQLLHSVE RFSQALQSGD
SPPLSFSQTN VQMSSMVIKS SHPETYQQRF VFPYFDLWGN VVIDKSYLEN LQSDSSIVTM
AFPTLQAILA QDIQENNFAE SLVMTTTVSH NTTMPFRISM TFKNNSPSGG ETKCVFWNFR
LANNTGGWDS SGCYVEEGDG DNVTCICDHL TSFSILMSPD SPDPSSLLGI LLDIISYVGV
GFSILSLAAC LVVEAVVWKS VTKNRTSYMR HTCIVNIAAS LLVANTWFIV VAAIQDNRYI
LCKTACVAAT FFIHFFYLSV FFWMLTLGLM LFYRLVFILH ETSRSTQKAI AFCLGYGCPL
AISVITLGAT QPREVYTRKN VCWLNWEDTK ALLAFAIPAL IIVVVNITIT IVVITKILRP
SIGDKPCKQE KSSLFQISKS IGVLTPLLGL TWGFGLTTVF PGTNLVFHII FAILNVFQGL
FILLFGCLWD LKVQEALLNK FSLSRWSSQH SKSTSLGSST PVFSMSSPIS RRFNNLFGKT
GTYNVSTPEA TSSSLENSSS ASSLLN
