ID AGRF1_HUMAN Reviewed; 910 AA. AC Q5T601; Q5KU15; Q5T5Z9; Q5T600; Q86SM1; Q8IXE3; Q8IZF8; Q96DQ1; Q9H615; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 10-AUG-2010, sequence version 2. DT 27-MAR-2024, entry version 162. DE RecName: Full=Adhesion G-protein coupled receptor F1 {ECO:0000303|PubMed:25713288}; DE AltName: Full=G protein-coupled receptor 110; DE AltName: Full=G protein-coupled receptor KPG_012; DE AltName: Full=G protein-coupled receptor PGR19; DE Flags: Precursor; GN Name=ADGRF1 {ECO:0000312|HGNC:HGNC:18990}; Synonyms=GPR110, PGR19; 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 [GENOMIC DNA]. RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.; RT "Genome-wide discovery and analysis of human seven transmembrane helix RT receptor genes."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Okazaki H., Inoue S., Yoshida S., Urakawa I., Mizutani S.; RT "Probable G-protein coupled receptor KPG_012."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 310-613 (ISOFORM 1). RC TISSUE=Small intestine, and Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 198-910 (ISOFORM 1). 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 460-636 (ISOFORM 1). 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 TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION. RX PubMed=20149256; DOI=10.1186/1471-2407-10-40; RA Lum A.M., Wang B.B., Beck-Engeser G.B., Li L., Channa N., Wabl M.; RT "Orphan receptor GPR110, an oncogene overexpressed in lung and prostate RT cancer."; RL BMC Cancer 10:40-40(2010). 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: Orphan receptor. CC -!- INTERACTION: CC Q5T601; P50148: GNAQ; NbExp=2; IntAct=EBI-46447105, EBI-3909604; CC Q5T601; Q5JWF2: GNAS; NbExp=2; IntAct=EBI-46447105, EBI-4400880; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20149256}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted CC {ECO:0000269|PubMed:20149256}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5T601-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5T601-2; Sequence=VSP_039588, VSP_039589; CC -!- TISSUE SPECIFICITY: Mainly expressed in the kidney. Up-regulated in CC lung adenocarcinomas and prostate cancers. CC {ECO:0000269|PubMed:20149256}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:20149256}. 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=BAB70874.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB70874.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305}; CC Sequence=BAC45260.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI13873.1; Type=Erroneous gene model prediction; Evidence={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; AB065679; BAC45260.1; ALT_SEQ; Genomic_DNA. DR EMBL; AB045123; BAD83599.1; -; mRNA. DR EMBL; AK026337; BAB15452.1; -; mRNA. DR EMBL; AK055208; BAB70874.1; ALT_SEQ; mRNA. DR EMBL; AL355518; CAI13873.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL355518; CAI13874.1; -; Genomic_DNA. DR EMBL; AL355518; CAI13875.1; -; Genomic_DNA. DR EMBL; CH471081; EAX04311.1; -; Genomic_DNA. DR EMBL; BC113634; AAI13635.1; -; mRNA. DR EMBL; BC113636; AAI13637.1; -; mRNA. DR EMBL; AY140952; AAN46666.1; -; mRNA. DR EMBL; AY255595; AAO85107.1; -; mRNA. DR CCDS; CCDS34471.1; -. [Q5T601-1] DR CCDS; CCDS4920.1; -. [Q5T601-2] DR RefSeq; NP_079324.2; NM_025048.3. [Q5T601-2] DR RefSeq; NP_722582.2; NM_153840.3. [Q5T601-1] DR PDB; 7WU3; EM; 3.10 A; R=251-860. DR PDB; 7WU4; EM; 3.40 A; R=251-860. DR PDB; 7WU5; EM; 3.00 A; R=251-860. DR PDB; 7WXU; EM; 2.85 A; R=1-910. DR PDB; 7WXW; EM; 2.84 A; R=1-910. DR PDB; 7WY0; EM; 2.83 A; R=1-910. DR PDB; 7WZ7; EM; 2.83 A; R=1-910. DR PDB; 7X2V; EM; 3.09 A; R=1-910. DR PDBsum; 7WU3; -. DR PDBsum; 7WU4; -. DR PDBsum; 7WU5; -. DR PDBsum; 7WXU; -. DR PDBsum; 7WXW; -. DR PDBsum; 7WY0; -. DR PDBsum; 7WZ7; -. DR PDBsum; 7X2V; -. DR AlphaFoldDB; Q5T601; -. DR EMDB; EMD-29684; -. DR EMDB; EMD-32818; -. DR EMDB; EMD-32819; -. DR EMDB; EMD-32820; -. DR EMDB; EMD-32881; -. DR EMDB; EMD-32882; -. DR EMDB; EMD-32883; -. DR EMDB; EMD-32905; -. DR EMDB; EMD-32972; -. DR SMR; Q5T601; -. DR BioGRID; 129353; 100. DR IntAct; Q5T601; 2. DR MINT; Q5T601; -. DR STRING; 9606.ENSP00000360299; -. DR ChEMBL; CHEMBL4523872; -. DR MEROPS; P02.022; -. DR MEROPS; P02.026; -. DR GlyCosmos; Q5T601; 19 sites, No reported glycans. DR GlyGen; Q5T601; 19 sites. DR iPTMnet; Q5T601; -. DR PhosphoSitePlus; Q5T601; -. DR BioMuta; ADGRF1; -. DR DMDM; 302393689; -. DR EPD; Q5T601; -. DR jPOST; Q5T601; -. DR MassIVE; Q5T601; -. DR PaxDb; 9606-ENSP00000360299; -. DR PeptideAtlas; Q5T601; -. DR ProteomicsDB; 64561; -. [Q5T601-1] DR ProteomicsDB; 64562; -. [Q5T601-2] DR Antibodypedia; 30773; 246 antibodies from 27 providers. DR DNASU; 266977; -. DR Ensembl; ENST00000371243.2; ENSP00000360289.2; ENSG00000153292.16. [Q5T601-2] DR Ensembl; ENST00000371253.7; ENSP00000360299.2; ENSG00000153292.16. [Q5T601-1] DR GeneID; 266977; -. DR KEGG; hsa:266977; -. DR MANE-Select; ENST00000371253.7; ENSP00000360299.2; NM_153840.4; NP_722582.2. DR UCSC; uc003oyt.4; human. [Q5T601-1] DR AGR; HGNC:18990; -. DR CTD; 266977; -. DR DisGeNET; 266977; -. DR GeneCards; ADGRF1; -. DR HGNC; HGNC:18990; ADGRF1. DR HPA; ENSG00000153292; Group enriched (esophagus, kidney, urinary bladder). DR MIM; 617430; gene. DR neXtProt; NX_Q5T601; -. DR OpenTargets; ENSG00000153292; -. DR PharmGKB; PA128394769; -. DR VEuPathDB; HostDB:ENSG00000153292; -. DR eggNOG; KOG4193; Eukaryota. DR GeneTree; ENSGT00940000161228; -. DR InParanoid; Q5T601; -. DR OMA; TQFLSTE; -. DR OrthoDB; 3876300at2759; -. DR PhylomeDB; Q5T601; -. DR TreeFam; TF316380; -. DR PathwayCommons; Q5T601; -. DR BioGRID-ORCS; 266977; 10 hits in 1147 CRISPR screens. DR ChiTaRS; ADGRF1; human. DR GeneWiki; GPR110; -. DR GenomeRNAi; 266977; -. DR Pharos; Q5T601; Tbio. DR PRO; PR:Q5T601; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q5T601; Protein. DR Bgee; ENSG00000153292; Expressed in palpebral conjunctiva and 97 other cell types or tissues. DR ExpressionAtlas; Q5T601; baseline and differential. DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; TAS:GDB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. 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:0045444; P:fat cell differentiation; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central. DR GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central. DR GO; GO:0007416; P:synapse assembly; IBA:GO_Central. DR CDD; cd15932; 7tmB2_GPR116-like_Adhesion_VI; 1. DR Gene3D; 1.25.40.610; -; 1. DR Gene3D; 2.60.220.50; -; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. 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; IPR000203; GPS. DR InterPro; IPR000082; SEA_dom. DR PANTHER; PTHR45813:SF3; ADHESION G-PROTEIN COUPLED RECEPTOR F1; 1. DR PANTHER; PTHR45813; EF-HAND DOMAIN-CONTAINING PROTEIN; 1. 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 PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1. DR PROSITE; PS50221; GPS; 1. DR PROSITE; PS50024; SEA; 1. DR Genevisible; Q5T601; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Secreted; Signal; Transducer; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..910 FT /note="Adhesion G-protein coupled receptor F1" FT /id="PRO_0000012891" FT TOPO_DOM 20..590 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 591..611 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 612..624 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 625..645 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 646..660 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 661..681 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 682..699 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 700..720 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 721..744 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 745..765 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 766..791 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 792..812 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 813..820 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 821..841 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 842..910 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 148..256 FT /note="SEA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188" FT DOMAIN 531..578 FT /note="GPS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 205 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 282 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 310 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 317 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 329 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 354 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 368 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 389 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 410 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 423 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 437 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 455 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 512 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 528 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 553 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 736 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 739 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 205..218 FT /note="NGSIVAGYEVVGSS -> MSLLSPKLECNGTI (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_039588" FT VAR_SEQ 219..910 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_039589" FT VARIANT 787 FT /note="I -> V (in dbSNP:rs1226475)" FT /id="VAR_055928" FT CONFLICT 23 FT /note="G -> GV (in Ref. 4; CAI13874)" FT /evidence="ECO:0000305" FT CONFLICT 27 FT /note="G -> D (in Ref. 3; BAB15452)" FT /evidence="ECO:0000305" FT CONFLICT 198..203 FT /note="VQVTQF -> MDISIQ (in Ref. 7; AAN46666)" FT /evidence="ECO:0000305" FT CONFLICT 614 FT /note="I -> A (in Ref. 3; BAB70874)" FT /evidence="ECO:0000305" FT HELIX 569..572 FT /evidence="ECO:0007829|PDB:7WY0" FT TURN 579..581 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 582..609 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 611..613 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 618..646 FT /evidence="ECO:0007829|PDB:7WY0" FT TURN 649..651 FT /evidence="ECO:0007829|PDB:7WY0" FT STRAND 653..655 FT /evidence="ECO:0007829|PDB:7WY0" FT TURN 656..658 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 659..686 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 695..706 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 708..721 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 722..724 FT /evidence="ECO:0007829|PDB:7WY0" FT STRAND 727..729 FT /evidence="ECO:0007829|PDB:7WU4" FT STRAND 730..734 FT /evidence="ECO:0007829|PDB:7WY0" FT STRAND 738..740 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 743..746 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 748..769 FT /evidence="ECO:0007829|PDB:7WY0" FT STRAND 774..777 FT /evidence="ECO:0007829|PDB:7WU3" FT STRAND 781..783 FT /evidence="ECO:0007829|PDB:7WU5" FT HELIX 785..799 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 803..806 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 807..812 FT /evidence="ECO:0007829|PDB:7WY0" FT TURN 816..818 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 820..827 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 830..837 FT /evidence="ECO:0007829|PDB:7WY0" FT TURN 838..841 FT /evidence="ECO:0007829|PDB:7WY0" FT HELIX 843..853 FT /evidence="ECO:0007829|PDB:7WY0" SQ SEQUENCE 910 AA; 101365 MW; 07B5234A487E9F07 CRC64; MKVGVLWLIS FFTFTDGHGG FLGKNDGIKT KKELIVNKKK HLGPVEEYQL LLQVTYRDSK EKRDLRNFLK LLKPPLLWSH GLIRIIRAKA TTDCNSLNGV LQCTCEDSYT WFPPSCLDPQ NCYLHTAGAL PSCECHLNNL SQSVNFCERT KIWGTFKINE RFTNDLLNSS SAIYSKYANG IEIQLKKAYE RIQGFESVQV TQFRNGSIVA GYEVVGSSSA SELLSAIEHV AEKAKTALHK LFPLEDGSFR VFGKAQCNDI VFGFGSKDDE YTLPCSSGYR GNITAKCESS GWQVIRETCV LSLLEELNKN FSMIVGNATE AAVSSFVQNL SVIIRQNPST TVGNLASVVS ILSNISSLSL ASHFRVSNST MEDVISIADN ILNSASVTNW TVLLREEKYA SSRLLETLEN ISTLVPPTAL PLNFSRKFID WKGIPVNKSQ LKRGYSYQIK MCPQNTSIPI RGRVLIGSDQ FQRSLPETII SMASLTLGNI LPVSKNGNAQ VNGPVISTVI QNYSINEVFL FFSKIESNLS QPHCVFWDFS HLQWNDAGCH LVNETQDIVT CQCTHLTSFS ILMSPFVPST IFPVVKWITY VGLGISIGSL ILCLIIEALF WKQIKKSQTS HTRRICMVNI ALSLLIADVW FIVGATVDTT VNPSGVCTAA VFFTHFFYLS LFFWMLMLGI LLAYRIILVF HHMAQHLMMA VGFCLGYGCP LIISVITIAV TQPSNTYKRK DVCWLNWSNG SKPLLAFVVP ALAIVAVNFV VVLLVLTKLW RPTVGERLSR DDKATIIRVG KSLLILTPLL GLTWGFGIGT IVDSQNLAWH VIFALLNAFQ GFFILCFGIL LDSKLRQLLF NKLSALSSWK QTEKQNSSDL SAKPKFSKPF NPLQNKGHYA FSHTGDSSDN IMLTQFVSNE //