IRAG2_HUMAN
ID IRAG2_HUMAN Reviewed; 555 AA.
AC Q12912; A0AVM2; B4E077; Q8N301;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Inositol 1,4,5-triphosphate receptor associated 2 {ECO:0000305};
DE AltName: Full=Lymphoid-restricted membrane protein;
DE AltName: Full=Protein Jaw1;
DE Contains:
DE RecName: Full=Processed inositol 1,4,5-triphosphate receptor associated 2;
GN Name=IRAG2 {ECO:0000312|HGNC:HGNC:6690}; Synonyms=JAW1, LRMP;
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 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANTS VAL-197; TRP-241 AND SER-253.
RX PubMed=8021504;
RA Behrens T.W., Jagadeesh J., Scherle P., Kearns G., Yewdell J., Staudt L.M.;
RT "Jaw1, a lymphoid-restricted membrane protein localized to the endoplasmic
RT reticulum.";
RL J. Immunol. 153:682-690(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-197.
RC TISSUE=Thymus;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-197
RP AND SER-253.
RC TISSUE=Brain, and Testis;
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 [5]
RP PROTEIN SEQUENCE OF 165-193; 209-216; 223-230; 283-290; 295-306; 310-322;
RP 345-358; 374-381; 422-435 AND 470-487, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16739114; DOI=10.1002/path.2002;
RA Tedoldi S., Paterson J.C., Cordell J., Tan S.Y., Jones M., Manek S.,
RA Dei Tos A.P., Roberton H., Masir N., Natkunam Y., Pileri S.A.,
RA Facchetti F., Hansmann M.L., Mason D.Y., Marafioti T.;
RT "Jaw1/LRMP, a germinal centre-associated marker for the immunohistological
RT study of B-cell lymphomas.";
RL J. Pathol. 209:454-463(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND SER-370, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91, 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 in the delivery of peptides to major
CC histocompatibility complex (MHC) class I molecules; this occurs in a
CC transporter associated with antigen processing (TAP)-independent
CC manner. May play a role in taste signal transduction via ITPR3. May
CC play a role during fertilization in pronucleus congression and fusion.
CC Plays a role in maintaining nuclear shape, maybe as a component of the
CC LINC complex and through interaction with microtubules.
CC {ECO:0000250|UniProtKB:Q60664}.
CC -!- SUBUNIT: Interacts (via coiled-coil domain) with ITPR3. Interacts with
CC SUN1 and SUN2. Interacts with microtubules.
CC {ECO:0000250|UniProtKB:Q60664}.
CC -!- SUBCELLULAR LOCATION: [Processed inositol 1,4,5-triphosphate receptor
CC associated 2]: Cytoplasm {ECO:0000250|UniProtKB:Q60664}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q60664}; Single-pass type IV membrane protein
CC {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q60664}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q5RHB5}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q5RHB5}. Chromosome
CC {ECO:0000250|UniProtKB:Q5RHB5}. Note=Colocalized with ITPR3 on the
CC endoplasmic reticulum membrane. {ECO:0000250|UniProtKB:Q60664}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12912-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12912-2; Sequence=VSP_036471;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in pre B-cells, mature B-
CC cells and pre T-cells. Expressed at low levels in mature T-cells and
CC plasma B-cells. Expressed in germinal center B-cells, splenic marginal
CC zone cells and B-cell lymphomas. Expressed in neuronal cells in the
CC cerebral cortex, epithelial cells in tonsil, adrenal glands, zymogen-
CC producing cells in the stomach and epithelial cells in seminal
CC vesicles. {ECO:0000269|PubMed:16739114, ECO:0000269|PubMed:8021504}.
CC -!- PTM: The removal of the C-terminal lumenal domain occurs by proteolytic
CC processing. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IRAG2 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-57 is the initiator
CC methionine. However, according to PubMed:8021504, the initiator
CC methionine is coded by a non-canonical CTG leucine codon; This leucine
CC codon is in an excellent Kozak consensus located 39 bp upstream of the
CC corresponding first mouse ATG. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29391.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAI26418.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U10485; AAA21604.1; -; mRNA.
DR EMBL; AK303256; BAG64339.1; -; mRNA.
DR EMBL; AC023510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029391; AAH29391.1; ALT_SEQ; mRNA.
DR EMBL; BC126417; AAI26418.1; ALT_INIT; mRNA.
DR CCDS; CCDS8701.1; -. [Q12912-2]
DR PIR; I38656; I38656.
DR RefSeq; NP_001191055.1; NM_001204126.1. [Q12912-2]
DR RefSeq; NP_001191056.1; NM_001204127.1. [Q12912-2]
DR RefSeq; NP_006143.2; NM_006152.3. [Q12912-2]
DR RefSeq; XP_005253427.1; XM_005253370.3.
DR RefSeq; XP_005253429.1; XM_005253372.2.
DR RefSeq; XP_005253431.1; XM_005253374.3.
DR RefSeq; XP_006719139.1; XM_006719076.2.
DR RefSeq; XP_011518969.1; XM_011520667.1.
DR RefSeq; XP_016874789.1; XM_017019300.1.
DR RefSeq; XP_016874790.1; XM_017019301.1.
DR RefSeq; XP_016874791.1; XM_017019302.1.
DR AlphaFoldDB; Q12912; -.
DR SMR; Q12912; -.
DR BioGRID; 110213; 9.
DR IntAct; Q12912; 7.
DR STRING; 9606.ENSP00000346442; -.
DR TCDB; 8.A.140.1.1; the lymphoid-restricted membrane protein (lrmp) family.
DR iPTMnet; Q12912; -.
DR MetOSite; Q12912; -.
DR PhosphoSitePlus; Q12912; -.
DR BioMuta; LRMP; -.
DR DMDM; 317373427; -.
DR EPD; Q12912; -.
DR jPOST; Q12912; -.
DR MassIVE; Q12912; -.
DR MaxQB; Q12912; -.
DR PaxDb; Q12912; -.
DR PeptideAtlas; Q12912; -.
DR PRIDE; Q12912; -.
DR ProteomicsDB; 59022; -. [Q12912-1]
DR ProteomicsDB; 59023; -. [Q12912-2]
DR Antibodypedia; 1183; 92 antibodies from 23 providers.
DR DNASU; 4033; -.
DR Ensembl; ENST00000354454.7; ENSP00000346442.3; ENSG00000118308.16. [Q12912-2]
DR Ensembl; ENST00000547044.5; ENSP00000450246.1; ENSG00000118308.16. [Q12912-2]
DR Ensembl; ENST00000548766.5; ENSP00000446496.1; ENSG00000118308.16. [Q12912-2]
DR Ensembl; ENST00000556887.6; ENSP00000451048.2; ENSG00000118308.16. [Q12912-2]
DR Ensembl; ENST00000557489.6; ENSP00000452116.2; ENSG00000118308.16. [Q12912-2]
DR GeneID; 4033; -.
DR KEGG; hsa:4033; -.
DR MANE-Select; ENST00000556887.6; ENSP00000451048.2; NM_001366544.2; NP_001353473.1. [Q12912-2]
DR UCSC; uc001rgh.4; human. [Q12912-1]
DR CTD; 4033; -.
DR DisGeNET; 4033; -.
DR GeneCards; IRAG2; -.
DR HGNC; HGNC:6690; IRAG2.
DR HPA; ENSG00000118308; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 602003; gene.
DR neXtProt; NX_Q12912; -.
DR OpenTargets; ENSG00000118308; -.
DR PharmGKB; PA30450; -.
DR VEuPathDB; HostDB:ENSG00000118308; -.
DR eggNOG; ENOG502QTH4; Eukaryota.
DR GeneTree; ENSGT00530000063722; -.
DR InParanoid; Q12912; -.
DR OMA; PTPDSHW; -.
DR OrthoDB; 560334at2759; -.
DR PhylomeDB; Q12912; -.
DR TreeFam; TF331789; -.
DR PathwayCommons; Q12912; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q12912; -.
DR BioGRID-ORCS; 4033; 14 hits in 1074 CRISPR screens.
DR ChiTaRS; LRMP; human.
DR GenomeRNAi; 4033; -.
DR Pharos; Q12912; Tbio.
DR PRO; PR:Q12912; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q12912; protein.
DR Bgee; ENSG00000118308; Expressed in secondary oocyte and 167 other tissues.
DR ExpressionAtlas; Q12912; baseline and differential.
DR Genevisible; Q12912; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0006997; P:nucleus organization; ISS:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR GO; GO:0006906; P:vesicle fusion; TAS:ProtInc.
DR GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
DR InterPro; IPR008677; MRVI1.
DR PANTHER; PTHR15352; PTHR15352; 1.
DR Pfam; PF05781; MRVI1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Endoplasmic reticulum; Fertilization; Immunity;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..555
FT /note="Inositol 1,4,5-triphosphate receptor associated 2"
FT /id="PRO_0000084483"
FT CHAIN 1..?
FT /note="Processed inositol 1,4,5-triphosphate receptor
FT associated 2"
FT /id="PRO_0000296244"
FT TOPO_DOM 1..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..555
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 84..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..341
FT /evidence="ECO:0000255"
FT COMPBIAS 131..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60664"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036471"
FT VARIANT 94
FT /note="T -> A (in dbSNP:rs6487451)"
FT /id="VAR_054545"
FT VARIANT 197
FT /note="L -> V (in dbSNP:rs7969931)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8021504"
FT /id="VAR_054546"
FT VARIANT 241
FT /note="L -> W (in dbSNP:rs1063159)"
FT /evidence="ECO:0000269|PubMed:8021504"
FT /id="VAR_054547"
FT VARIANT 253
FT /note="C -> S (in dbSNP:rs1908946)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8021504"
FT /id="VAR_054548"
FT CONFLICT 81
FT /note="E -> G (in Ref. 1; AAA21604)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="C -> R (in Ref. 2; BAG64339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 62122 MW; FAFA4B94DCEB1A42 CRC64;
MESTPFSGVA NQIHTLCERP TYGEVKDGAL DVKRQHKCPG PTSGPSPGTN LSGCIRMNDD
PSMEENGVER VCPESLLQSR EYSSLPLPRH TSSTDGTITS SDPGLEILNM ASCDLDRNSL
CKKEEDTRSA SPTIEAQGTS PAHDNIAFQD STSKDKTILN LEAKEEPETI EEHKKEHASG
DSVVSPLPVT TVKSVNLRQS ENTSANEKEV EAEFLRLSLG FKCDWFTLEK RVKLEERSRD
LAEENLKKEI TNCLKLLESL TPLCEDDNQA QEIIKKLEKS IKFLSQCAAR VASRAEMLGA
INQESRVSKA VEVMIQHVEN LKRMYAKEHA ELEELKQVLL QNERSFNPLE DDDDCQIKKR
SASLNSKPSS LRRVTIASLP RNIGNAGMVA GMENNDRFSR RSSSWRILGS KQSEHRPSLP
RFISTYSWAD AEEEKCELKT KDDSEPSGEE TVERTRKPSL SEKKNNPSKW DVSSVYDTIA
SWATNLKSSI RKANKALWLS IAFIVLFAAL MSFLTGQLFQ KSVDAAPTQQ EDSWTSLEHI
LWPFTRLRHN GPPPV
