IRAG1_HUMAN
ID IRAG1_HUMAN Reviewed; 904 AA.
AC Q9Y6F6; B7Z3T4; B7Z6I2; B7Z9A3; E9PQY6; F5H6A1; J3KQZ7; Q17S00; Q9UNY1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Inositol 1,4,5-triphosphate receptor associated 1 {ECO:0000305};
DE AltName: Full=Inositol 1,4,5-trisphosphate receptor-associated cGMP kinase substrate;
DE AltName: Full=JAW1-related protein MRVI1;
DE AltName: Full=Protein MRVI1;
GN Name=IRAG1 {ECO:0000312|HGNC:HGNC:7237}; Synonyms=IRAG, JAW1L, MRVI1;
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] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, AND
RP VARIANTS VAL-11 AND THR-70.
RX PubMed=10321731; DOI=10.1038/sj.onc.1202419;
RA Shaughnessy J.D. Jr., Largaespada D.A., Tian E., Fletcher C.F., Cho B.C.,
RA Vyas P., Jenkins N.A., Copeland N.G.;
RT "Mrvi1, a common MRV integration site in BXH2 myeloid leukemias, encodes a
RT protein with homology to a lymphoid-restricted membrane protein Jaw1.";
RL Oncogene 18:2069-2084(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7; 8 AND 9), AND VARIANTS
RP VAL-11 AND THR-70.
RC TISSUE=Placenta, Thalamus, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Brain;
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 [6]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=14729908; DOI=10.1074/jbc.m313365200;
RA Fritsch R.M., Saur D., Kurjak M., Oesterle D., Schlossmann J.,
RA Geiselhoeringer A., Hofmann F., Allescher H.-D.;
RT "InsP3R-associated cGMP kinase substrate (IRAG) is essential for nitric
RT oxide-induced inhibition of calcium signaling in human colonic smooth
RT muscle.";
RL J. Biol. Chem. 279:12551-12559(2004).
RN [7]
RP INTERACTION WITH PRKG1 AND ITPR1, AND PHOSPHORYLATION AT SER-386; SER-676
RP AND SER-689.
RX PubMed=16990611; DOI=10.1182/blood-2005-10-026294;
RA Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I., Kocher T.,
RA Wilm M., Hofmann F., Massberg S., Schlossmann J.;
RT "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and
RT thrombus formation.";
RL Blood 109:552-559(2007).
RN [8]
RP INDUCTION BY BTF3.
RX PubMed=17312387; DOI=10.4161/cbt.6.3.3704;
RA Kusumawidjaja G., Kayed H., Giese N., Bauer A., Erkan M., Giese T.,
RA Hoheise J.D., Friess H., Kleeff J.;
RT "Basic transcription factor 3 (BTF3) regulates transcription of tumor-
RT associated genes in pancreatic cancer cells.";
RL Cancer Biol. Ther. 6:367-376(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386, 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: Plays a role as NO/PRKG1-dependent regulator of IP3-induced
CC calcium release; its phosphorylation by PRKG1 inhibits bradykinin and
CC IP3-induced calcium release from intracellular stores. Recruits PRKG1
CC to the endoplasmic reticulum and may mediate the assembly of PRKG1 and
CC ITPR1 in a macrocomplex. Involved in PRKG1 signaling cascade leading to
CC inhibition of platelet activation and aggregation. Mediates also NO-
CC dependent inhibition of calcium signaling in gastrointestinal smooth
CC muscle contributing to NO-dependent relaxation.
CC {ECO:0000269|PubMed:14729908}.
CC -!- SUBUNIT: Part of cGMP kinase signaling complex at least composed of
CC ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1
CC (By similarity). Interacts with PRKG1/cGKI-beta and ITPR1/IP3R type I.
CC {ECO:0000250, ECO:0000269|PubMed:16990611}.
CC -!- INTERACTION:
CC Q9Y6F6-3; P07339: CTSD; NbExp=3; IntAct=EBI-25840037, EBI-2115097;
CC Q9Y6F6-3; P28799: GRN; NbExp=3; IntAct=EBI-25840037, EBI-747754;
CC Q9Y6F6-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25840037, EBI-5235340;
CC Q9Y6F6-3; O76024: WFS1; NbExp=3; IntAct=EBI-25840037, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Sarcoplasmic
CC reticulum {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=9;
CC IsoId=Q9Y6F6-9; Sequence=Displayed;
CC Name=2; Synonyms=IRAG1A;
CC IsoId=Q9Y6F6-2; Sequence=VSP_028342, VSP_059441;
CC Name=3; Synonyms=IRAG1B;
CC IsoId=Q9Y6F6-3; Sequence=VSP_028341, VSP_059441;
CC Name=4;
CC IsoId=Q9Y6F6-4; Sequence=VSP_059442;
CC Name=5;
CC IsoId=Q9Y6F6-5; Sequence=VSP_028341, VSP_059442;
CC Name=6;
CC IsoId=Q9Y6F6-6; Sequence=VSP_040452;
CC Name=7;
CC IsoId=Q9Y6F6-7; Sequence=VSP_046361, VSP_059442;
CC Name=8;
CC IsoId=Q9Y6F6-8; Sequence=VSP_046361, VSP_059442, VSP_046362,
CC VSP_046363;
CC Name=1;
CC IsoId=Q9Y6F6-1; Sequence=VSP_059440;
CC -!- TISSUE SPECIFICITY: Expressed in the colon, rectum, and cultured
CC colonic smooth muscle. Detected in various cancer cell lines.
CC {ECO:0000269|PubMed:10321731, ECO:0000269|PubMed:14729908}.
CC -!- INDUCTION: By silencing of the transcription factor BTF3.
CC {ECO:0000269|PubMed:17312387}.
CC -!- PTM: Phosphorylated by PRKG1/cGKI-beta; Ser-386 showed constitutive
CC phosphorylation in platelets whereas Ser-676 is only phosphorylated in
CC presence of cGMP and nitric oxide (NO); Ser-689 is phosphorylated in
CC resting platelets but increases in presence of cGMP and NO. PRKG1
CC inhibitor prevents phosphorylation of Ser-676 and Ser-689 in response
CC to NO and cGMP. {ECO:0000269|PubMed:16990611}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD25922.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD25923.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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DR EMBL; AF081249; AAD25922.1; ALT_FRAME; mRNA.
DR EMBL; AF081250; AAD25923.1; ALT_SEQ; mRNA.
DR EMBL; AK296336; BAH12320.1; -; mRNA.
DR EMBL; AK300358; BAH13268.1; -; mRNA.
DR EMBL; AK304702; BAH14239.1; -; mRNA.
DR EMBL; AC009532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68559.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68560.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68561.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68562.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68563.1; -; Genomic_DNA.
DR EMBL; BC117127; AAI17128.1; -; mRNA.
DR CCDS; CCDS44538.2; -. [Q9Y6F6-9]
DR CCDS; CCDS44539.1; -. [Q9Y6F6-5]
DR CCDS; CCDS44540.1; -. [Q9Y6F6-6]
DR CCDS; CCDS55745.1; -. [Q9Y6F6-8]
DR CCDS; CCDS55746.1; -. [Q9Y6F6-7]
DR RefSeq; NP_001092049.2; NM_001098579.2. [Q9Y6F6-9]
DR RefSeq; NP_001093633.1; NM_001100163.2. [Q9Y6F6-5]
DR RefSeq; NP_001093637.1; NM_001100167.2. [Q9Y6F6-6]
DR RefSeq; NP_001193809.1; NM_001206880.1. [Q9Y6F6-8]
DR RefSeq; NP_001193810.1; NM_001206881.1. [Q9Y6F6-6]
DR RefSeq; NP_569056.4; NM_130385.3. [Q9Y6F6-7]
DR AlphaFoldDB; Q9Y6F6; -.
DR SMR; Q9Y6F6; -.
DR BioGRID; 115617; 13.
DR IntAct; Q9Y6F6; 9.
DR MINT; Q9Y6F6; -.
DR STRING; 9606.ENSP00000412130; -.
DR iPTMnet; Q9Y6F6; -.
DR PhosphoSitePlus; Q9Y6F6; -.
DR BioMuta; MRVI1; -.
DR DMDM; 158706131; -.
DR jPOST; Q9Y6F6; -.
DR MassIVE; Q9Y6F6; -.
DR PaxDb; Q9Y6F6; -.
DR PeptideAtlas; Q9Y6F6; -.
DR PRIDE; Q9Y6F6; -.
DR ProteomicsDB; 23158; -.
DR ProteomicsDB; 27125; -.
DR ProteomicsDB; 86663; -. [Q9Y6F6-1]
DR ProteomicsDB; 86664; -. [Q9Y6F6-2]
DR ProteomicsDB; 86665; -. [Q9Y6F6-3]
DR ProteomicsDB; 86666; -. [Q9Y6F6-4]
DR ProteomicsDB; 86667; -. [Q9Y6F6-5]
DR ProteomicsDB; 86668; -. [Q9Y6F6-6]
DR Antibodypedia; 2234; 30 antibodies from 13 providers.
DR DNASU; 10335; -.
DR Ensembl; ENST00000423302.7; ENSP00000412130.2; ENSG00000072952.20. [Q9Y6F6-7]
DR Ensembl; ENST00000424001.5; ENSP00000401205.1; ENSG00000072952.20. [Q9Y6F6-6]
DR Ensembl; ENST00000527509.7; ENSP00000432067.3; ENSG00000072952.20. [Q9Y6F6-5]
DR Ensembl; ENST00000531107.5; ENSP00000432436.1; ENSG00000072952.20. [Q9Y6F6-9]
DR Ensembl; ENST00000534266.6; ENSP00000433296.2; ENSG00000072952.20. [Q9Y6F6-6]
DR Ensembl; ENST00000541483.5; ENSP00000437784.1; ENSG00000072952.20. [Q9Y6F6-8]
DR Ensembl; ENST00000547195.5; ENSP00000448278.2; ENSG00000072952.20. [Q9Y6F6-6]
DR Ensembl; ENST00000558540.5; ENSP00000453013.1; ENSG00000072952.20. [Q9Y6F6-6]
DR GeneID; 10335; -.
DR KEGG; hsa:10335; -.
DR MANE-Select; ENST00000423302.7; ENSP00000412130.2; NM_130385.4; NP_569056.4. [Q9Y6F6-7]
DR UCSC; uc001mix.4; human. [Q9Y6F6-9]
DR CTD; 10335; -.
DR DisGeNET; 10335; -.
DR GeneCards; IRAG1; -.
DR HGNC; HGNC:7237; IRAG1.
DR HPA; ENSG00000072952; Low tissue specificity.
DR MIM; 604673; gene.
DR neXtProt; NX_Q9Y6F6; -.
DR OpenTargets; ENSG00000072952; -.
DR PharmGKB; PA31032; -.
DR VEuPathDB; HostDB:ENSG00000072952; -.
DR eggNOG; ENOG502QWGQ; Eukaryota.
DR GeneTree; ENSGT00530000063722; -.
DR HOGENOM; CLU_018275_0_0_1; -.
DR InParanoid; Q9Y6F6; -.
DR OMA; MGVDLTC; -.
DR OrthoDB; 560334at2759; -.
DR PhylomeDB; Q9Y6F6; -.
DR TreeFam; TF331789; -.
DR PathwayCommons; Q9Y6F6; -.
DR Reactome; R-HSA-418457; cGMP effects.
DR SignaLink; Q9Y6F6; -.
DR SIGNOR; Q9Y6F6; -.
DR BioGRID-ORCS; 10335; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; MRVI1; human.
DR GeneWiki; MRVI1; -.
DR GenomeRNAi; 10335; -.
DR Pharos; Q9Y6F6; Tbio.
DR PRO; PR:Q9Y6F6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y6F6; protein.
DR Bgee; ENSG00000072952; Expressed in saphenous vein and 180 other tissues.
DR ExpressionAtlas; Q9Y6F6; baseline and differential.
DR Genevisible; Q9Y6F6; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031095; C:platelet dense tubular network membrane; TAS:Reactome.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR InterPro; IPR008677; MRVI1.
DR PANTHER; PTHR15352; PTHR15352; 1.
DR Pfam; PF05781; MRVI1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Sarcoplasmic reticulum; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..904
FT /note="Inositol 1,4,5-triphosphate receptor associated 1"
FT /id="PRO_0000305292"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 30..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..176
FT /note="Interaction with PRKG1"
FT /evidence="ECO:0000250"
FT REGION 166..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..573
FT /note="Interaction with ITPR1"
FT /evidence="ECO:0000250"
FT REGION 699..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 540..638
FT /evidence="ECO:0000255"
FT COMPBIAS 77..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..816
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9N1F0"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16990611,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16990611"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16990611"
FT VAR_SEQ 1..307
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040452"
FT VAR_SEQ 1..83
FT /note="MGMDLTCPFGISPACGAQASWSIFGADAAEVPGTRGHSQQEAAMPHIPEDEE
FT PPGEPQAAQSPAGQGPPAAGVSCSPTPTIVL -> M (in isoform 3 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028341"
FT VAR_SEQ 1..13
FT /note="MGMDLTCPFGISP -> MVKAPQSEERLARGGKENNSVL (in isoform
FT 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046361"
FT VAR_SEQ 65
FT /note="G -> GQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10321731"
FT /id="VSP_028342"
FT VAR_SEQ 209..228
FT /note="GLDVCSGPPSPLPGAPPQQK -> D (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_059440"
FT VAR_SEQ 209..228
FT /note="GLDVCSGPPSPLPGAPPQQK -> E (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:10321731"
FT /id="VSP_059441"
FT VAR_SEQ 227
FT /note="Missing (in isoform 4, isoform 5, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:10321731,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_059442"
FT VAR_SEQ 229..260
FT /note="GDEADVSSPHPGEPNVPKGLADRKQNDQRKVS -> GDEADVSSPHPGEP
FT (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046362"
FT VAR_SEQ 261..448
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046363"
FT VARIANT 11
FT /note="I -> V (in dbSNP:rs4909945)"
FT /evidence="ECO:0000269|PubMed:10321731,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_056942"
FT VARIANT 28
FT /note="A -> T (in dbSNP:rs34302310)"
FT /id="VAR_056943"
FT VARIANT 70
FT /note="A -> T (in dbSNP:rs2162044)"
FT /evidence="ECO:0000269|PubMed:10321731,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_056944"
FT VARIANT 186
FT /note="P -> S (in dbSNP:rs35857561)"
FT /id="VAR_056945"
FT VARIANT 289
FT /note="Q -> H (in dbSNP:rs34398944)"
FT /id="VAR_056946"
FT CONFLICT 42
FT /note="A -> G (in Ref. 1; AAD25922)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="P -> S (in Ref. 1; AAD25922)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="R -> M (in Ref. 2; BAH12320)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="S -> G (in Ref. 2; BAH12320)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="E -> G (in Ref. 2; BAH12320)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="P -> L (in Ref. 1; AAD25922/AAD25923)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="R -> K (in Ref. 1; AAD25922/AAD25923)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9Y6F6-7:9
FT /note="E -> G (in Ref. 2; BAH12320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 97957 MW; 94891F4B4807A61A CRC64;
MGMDLTCPFG ISPACGAQAS WSIFGADAAE VPGTRGHSQQ EAAMPHIPED EEPPGEPQAA
QSPAGQGPPA AGVSCSPTPT IVLTGDATSP EGETDKNLAN RVHSPHKRLS HRHLKVSTAS
LTSVDPAGHI IDLVNDQLPD ISISEEDKKK NLALLEEAKL VSERFLTRRG RKSRSSPGDS
PSAVSPNLSP SASPTSSRSN SLTVPTPPGL DVCSGPPSPL PGAPPQQKGD EADVSSPHPG
EPNVPKGLAD RKQNDQRKVS QGRLAPRPPP VEKSKEIAIE QKENFDPLQY PETTPKGLAP
VTNSSGKMAL NSPQPGPVES ELGKQLLKTG WEGSPLPRSP TQDAAGVGPP ASQGRGPAGE
PMGPEAGSKA ELPPTVSRPP LLRGLSWDSG PEEPGPRLQK VLAKLPLAEE EKRFAGKAGG
KLAKAPGLKD FQIQVQPVRM QKLTKLREEH ILMRNQNLVG LKLPDLSEAA EQEKGLPSEL
SPAIEEEESK SGLDVMPNIS DVLLRKLRVH RSLPGSAPPL TEKEVENVFV QLSLAFRNDS
YTLESRINQA ERERNLTEEN TEKELENFKA SITSSASLWH HCEHRETYQK LLEDIAVLHR
LAARLSSRAE VVGAVRQEKR MSKATEVMMQ YVENLKRTYE KDHAELMEFK KLANQNSSRS
CGPSEDGVPR TARSMSLTLG KNMPRRRVSV AVVPKFNALN LPGQTPSSSS IPSLPALSES
PNGKGSLPVT SALPALLENG KTNGDPDCEA SAPALTLSCL EELSQETKAR MEEEAYSKGF
QEGLKKTKEL QDLKEEEEEQ KSESPEEPEE VEETEEEEKG PRSSKLEELV HFLQVMYPKL
CQHWQVIWMM AAVMLVLTVV LGLYNSYNSC AEQADGPLGR STCSAAQRDS WWSSGLQHEQ
PTEQ
