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AGRF1_HUMAN
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   03-AUG-2022, entry version 153.
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   -!- 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};
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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   AlphaFoldDB; Q5T601; -.
DR   SMR; Q5T601; -.
DR   BioGRID; 129353; 100.
DR   STRING; 9606.ENSP00000360299; -.
DR   ChEMBL; CHEMBL4523872; -.
DR   MEROPS; P02.022; -.
DR   MEROPS; P02.026; -.
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; Q5T601; -.
DR   PeptideAtlas; Q5T601; -.
DR   PRIDE; Q5T601; -.
DR   ProteomicsDB; 64561; -. [Q5T601-1]
DR   ProteomicsDB; 64562; -. [Q5T601-2]
DR   Antibodypedia; 30773; 195 antibodies from 26 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   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; 611778at2759; -.
DR   PhylomeDB; Q5T601; -.
DR   TreeFam; TF316380; -.
DR   PathwayCommons; Q5T601; -.
DR   BioGRID-ORCS; 266977; 8 hits in 1069 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 95 other tissues.
DR   ExpressionAtlas; Q5T601; baseline and differential.
DR   Genevisible; Q5T601; HS.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; TAS:GDB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004949; F:cannabinoid receptor activity; IEA:Ensembl.
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: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:0032793; P:positive regulation of CREB transcription factor activity; IEA:Ensembl.
DR   GO; GO:0007416; P:synapse assembly; IBA:GO_Central.
DR   Gene3D; 2.60.220.50; -; 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; IPR000203; GPS.
DR   InterPro; IPR000082; SEA_dom.
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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Secreted; Signal;
KW   Transducer; Transmembrane; 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"
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
 
 
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