GPC5C_HUMAN
ID GPC5C_HUMAN Reviewed; 441 AA.
AC Q9NQ84; B5BUN4; Q2NL85; Q9NZG5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=G-protein coupled receptor family C group 5 member C;
DE AltName: Full=Retinoic acid-induced gene 3 protein;
DE Short=RAIG-3;
DE Flags: Precursor;
GN Name=GPRC5C; Synonyms=RAIG3; ORFNames=PSEC0087;
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), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=10945465; DOI=10.1006/geno.2000.6226;
RA Robbins M.J., Michalovich D., Hill J., Calver A.R., Medhurst A.D.,
RA Gloger I., Sims M.A., Middlemiss D.N., Pangalos M.N.;
RT "Molecular cloning and characterization of two novel retinoic acid-
RT inducible orphan G-protein-coupled receptors (GPRC5B and GPRC5C).";
RL Genomics 67:8-18(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=11311935; DOI=10.1016/s0167-4781(01)00197-x;
RA Braeuner-Osborne H., Jensen A.A., Sheppard P.O., Brodin B.,
RA Krogsgaard-Larsen P., O'Hara P.;
RT "Cloning and characterization of a human orphan family C G-protein coupled
RT receptor GPRC5D.";
RL Biochim. Biophys. Acta 1518:237-248(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary, and Pancreas;
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; SER-383 AND THR-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: This retinoic acid-inducible G-protein coupled receptor
CC provide evidence for a possible interaction between retinoid and G-
CC protein signaling pathways. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Cytoplasmic vesicle membrane; Multi-pass membrane protein.
CC Note=Localized in the plasma membrane and perinuclear vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NQ84-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQ84-2; Sequence=VSP_037725;
CC -!- TISSUE SPECIFICITY: Expression is highest in the periphery,
CC particularly in the stomach, but also in the kidney, liver, pancreas,
CC and prostate. In brain, levels of expression are generally lower than
CC in the periphery, with the exception of cerebellum, spinal cord, and
CC dorsal root ganglia (DRG). {ECO:0000269|PubMed:10945465,
CC ECO:0000269|PubMed:11311935}.
CC -!- INDUCTION: By all-trans retinoic acid (ATRA).
CC {ECO:0000269|PubMed:10945465, ECO:0000269|PubMed:11311935}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16860.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI10849.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI25081.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI25082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG54752.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC00633.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ276102; CAC00633.1; ALT_INIT; mRNA.
DR EMBL; AF207989; AAF72870.1; -; mRNA.
DR EMBL; BT007435; AAP36103.1; -; mRNA.
DR EMBL; AK131210; BAG54752.1; ALT_INIT; mRNA.
DR EMBL; AK075397; BAC11595.1; -; mRNA.
DR EMBL; AB451470; BAG70284.1; -; mRNA.
DR EMBL; AC079325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89163.1; -; Genomic_DNA.
DR EMBL; BC016860; AAH16860.2; ALT_INIT; mRNA.
DR EMBL; BC110848; AAI10849.1; ALT_INIT; mRNA.
DR EMBL; BC125080; AAI25081.1; ALT_INIT; mRNA.
DR EMBL; BC125081; AAI25082.1; ALT_INIT; mRNA.
DR CCDS; CCDS11699.1; -. [Q9NQ84-1]
DR CCDS; CCDS42378.1; -. [Q9NQ84-1]
DR RefSeq; NP_061123.3; NM_018653.3. [Q9NQ84-1]
DR RefSeq; NP_071319.2; NM_022036.2. [Q9NQ84-1]
DR AlphaFoldDB; Q9NQ84; -.
DR BioGRID; 120980; 128.
DR IntAct; Q9NQ84; 33.
DR STRING; 9606.ENSP00000376403; -.
DR ChEMBL; CHEMBL4523921; -.
DR TCDB; 9.A.14.11.2; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q9NQ84; 1 site.
DR iPTMnet; Q9NQ84; -.
DR PhosphoSitePlus; Q9NQ84; -.
DR SwissPalm; Q9NQ84; -.
DR BioMuta; GPRC5C; -.
DR DMDM; 46396014; -.
DR EPD; Q9NQ84; -.
DR jPOST; Q9NQ84; -.
DR MassIVE; Q9NQ84; -.
DR MaxQB; Q9NQ84; -.
DR PaxDb; Q9NQ84; -.
DR PeptideAtlas; Q9NQ84; -.
DR PRIDE; Q9NQ84; -.
DR ProteomicsDB; 82101; -. [Q9NQ84-1]
DR ProteomicsDB; 82102; -. [Q9NQ84-2]
DR Antibodypedia; 31968; 241 antibodies from 29 providers.
DR DNASU; 55890; -.
DR Ensembl; ENST00000392627.7; ENSP00000376403.2; ENSG00000170412.18. [Q9NQ84-1]
DR Ensembl; ENST00000392629.3; ENSP00000376405.3; ENSG00000170412.18. [Q9NQ84-1]
DR Ensembl; ENST00000652294.1; ENSP00000498839.1; ENSG00000170412.18. [Q9NQ84-2]
DR GeneID; 55890; -.
DR KEGG; hsa:55890; -.
DR MANE-Select; ENST00000392627.7; ENSP00000376403.2; NM_022036.4; NP_071319.3.
DR UCSC; uc002jkp.4; human. [Q9NQ84-1]
DR CTD; 55890; -.
DR DisGeNET; 55890; -.
DR GeneCards; GPRC5C; -.
DR HGNC; HGNC:13309; GPRC5C.
DR HPA; ENSG00000170412; Tissue enhanced (liver, stomach).
DR MIM; 605949; gene.
DR neXtProt; NX_Q9NQ84; -.
DR OpenTargets; ENSG00000170412; -.
DR PharmGKB; PA28939; -.
DR VEuPathDB; HostDB:ENSG00000170412; -.
DR eggNOG; ENOG502QQEH; Eukaryota.
DR GeneTree; ENSGT00950000182961; -.
DR HOGENOM; CLU_044162_1_1_1; -.
DR InParanoid; Q9NQ84; -.
DR OMA; TIPQICC; -.
DR OrthoDB; 807909at2759; -.
DR PhylomeDB; Q9NQ84; -.
DR TreeFam; TF321410; -.
DR PathwayCommons; Q9NQ84; -.
DR SignaLink; Q9NQ84; -.
DR BioGRID-ORCS; 55890; 8 hits in 1070 CRISPR screens.
DR ChiTaRS; GPRC5C; human.
DR GenomeRNAi; 55890; -.
DR Pharos; Q9NQ84; Tbio.
DR PRO; PR:Q9NQ84; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NQ84; protein.
DR Bgee; ENSG00000170412; Expressed in right lobe of liver and 145 other tissues.
DR ExpressionAtlas; Q9NQ84; baseline and differential.
DR Genevisible; Q9NQ84; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR InterPro; IPR017978; GPCR_3_C.
DR Pfam; PF00003; 7tm_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..441
FT /note="G-protein coupled receptor family C group 5 member
FT C"
FT /id="PRO_0000012967"
FT TOPO_DOM 24..50
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 412..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT MOD_RES 414
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT MOD_RES 423
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1
FT /note="M -> MGTQPEPGLGARM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10945465,
FT ECO:0000303|PubMed:19054851"
FT /id="VSP_037725"
FT CONFLICT 204
FT /note="I -> V (in Ref. 1; CAC00633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 48193 MW; B255D9680328FE3D CRC64;
MAIHKALVMC LGLPLFLFPG AWAQGHVPPG CSQGLNPLYY NLCDRSGAWG IVLEAVAGAG
IVTTFVLTII LVASLPFVQD TKKRSLLGTQ VFFLLGTLGL FCLVFACVVK PDFSTCASRR
FLFGVLFAIC FSCLAAHVFA LNFLARKNHG PRGWVIFTVA LLLTLVEVII NTEWLIITLV
RGSGEGGPQG NSSAGWAVAS PCAIANMDFV MALIYVMLLL LGAFLGAWPA LCGRYKRWRK
HGVFVLLTTA TSVAIWVVWI VMYTYGNKQH NSPTWDDPTL AIALAANAWA FVLFYVIPEV
SQVTKSSPEQ SYQGDMYPTR GVGYETILKE QKGQSMFVEN KAFSMDEPVA AKRPVSPYSG
YNGQLLTSVY QPTEMALMHK VPSEGAYDII LPRATANSQV MGSANSTLRA EDMYSAQSHQ
AATPPKDGKN SQVFRNPYVW D
