ANM7_HUMAN
ID ANM7_HUMAN Reviewed; 692 AA.
AC Q9NVM4; B3KPR0; B3KUG9; B4E379; Q96PV5; Q9H9L0;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Protein arginine N-methyltransferase 7;
DE EC=2.1.1.321 {ECO:0000269|PubMed:25294873};
DE AltName: Full=Histone-arginine N-methyltransferase PRMT7;
DE AltName: Full=[Myelin basic protein]-arginine N-methyltransferase PRMT7;
GN Name=PRMT7; Synonyms=KIAA1933;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain, Spleen, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-692 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [4]
RP FUNCTION.
RX PubMed=15044439; DOI=10.1074/jbc.m312904200;
RA Miranda T.B., Miranda M., Frankel A., Clarke S.;
RT "PRMT7 is a member of the protein arginine methyltransferase family with a
RT distinct substrate specificity.";
RL J. Biol. Chem. 279:22902-22907(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15494416; DOI=10.1074/jbc.m405295200;
RA Lee J.-H., Cook J.R., Yang Z.-H., Mirochnitchenko O., Gunderson S.I.,
RA Felix A.M., Herth N., Hoffmann R., Pestka S.;
RT "PRMT7, a new protein arginine methyltransferase that synthesizes symmetric
RT dimethylarginine.";
RL J. Biol. Chem. 280:3656-3664(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH PRMT5 AND SNRPD3.
RX PubMed=17709427; DOI=10.1083/jcb.200702147;
RA Gonsalvez G.B., Tian L., Ospina J.K., Boisvert F.-M., Lamond A.I.,
RA Matera A.G.;
RT "Two distinct arginine methyltransferases are required for biogenesis of
RT Sm-class ribonucleoproteins.";
RL J. Cell Biol. 178:733-740(2007).
RN [7]
RP INCREASED SENSITIVITY TO CAMPTOTHECIN.
RX PubMed=18381071; DOI=10.1016/j.febslet.2008.03.031;
RA Verbiest V., Montaudon D., Tautu M.T., Moukarzel J., Portail J.-P.,
RA Markovits J., Robert J., Ichas F., Pourquier P.;
RT "Protein arginine (N)-methyl transferase 7 (PRMT7) as a potential target
RT for the sensitization of tumor cells to camptothecins.";
RL FEBS Lett. 582:1483-1489(2008).
RN [8]
RP POSSIBLE INVOLVEMENT IN ETOPOSIDE-INDUCED CYTOTOXICITY.
RX PubMed=19089452; DOI=10.1007/s00439-008-0607-4;
RA Bleibel W.K., Duan S., Huang R.S., Kistner E.O., Shukla S.J., Wu X.,
RA Badner J.A., Dolan M.E.;
RT "Identification of genomic regions contributing to etoposide-induced
RT cytotoxicity.";
RL Hum. Genet. 125:173-180(2009).
RN [9]
RP FUNCTION.
RX PubMed=19110445; DOI=10.1016/j.jasms.2008.11.008;
RA Wang H., Straubinger R.M., Aletta J.M., Cao J., Duan X., Yu H., Qu J.;
RT "Accurate localization and relative quantification of arginine methylation
RT using nanoflow liquid chromatography coupled to electron transfer
RT dissociation and orbitrap mass spectrometry.";
RL J. Am. Soc. Mass Spectrom. 20:507-519(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP CATALYTIC ACTIVITY.
RX PubMed=25294873; DOI=10.1074/jbc.m114.609271;
RA Feng Y., Hadjikyriacou A., Clarke S.G.;
RT "Substrate specificity of human protein arginine methyltransferase 7
RT (PRMT7): the importance of acidic residues in the double E loop.";
RL J. Biol. Chem. 289:32604-32616(2014).
RN [12]
RP INVOLVEMENT IN SBIDDS, AND VARIANTS SBIDDS THR-32; GLY-387 AND ARG-494.
RX PubMed=26437029; DOI=10.1038/ng.3410;
RG DDD study;
RA Akawi N., McRae J., Ansari M., Balasubramanian M., Blyth M., Brady A.F.,
RA Clayton S., Cole T., Deshpande C., Fitzgerald T.W., Foulds N., Francis R.,
RA Gabriel G., Gerety S.S., Goodship J., Hobson E., Jones W.D., Joss S.,
RA King D., Klena N., Kumar A., Lees M., Lelliott C., Lord J., McMullan D.,
RA O'Regan M., Osio D., Piombo V., Prigmore E., Rajan D., Rosser E.,
RA Sifrim A., Smith A., Swaminathan G.J., Turnpenny P., Whitworth J.,
RA Wright C.F., Firth H.V., Barrett J.C., Lo C.W., FitzPatrick D.R.,
RA Hurles M.E.;
RT "Discovery of four recessive developmental disorders using probabilistic
RT genotype and phenotype matching among 4,125 families.";
RL Nat. Genet. 47:1363-1369(2015).
CC -!- FUNCTION: Arginine methyltransferase that can both catalyze the
CC formation of omega-N monomethylarginine (MMA) and symmetrical
CC dimethylarginine (sDMA), with a preference for the formation of MMA.
CC Specifically mediates the symmetrical dimethylation of arginine
CC residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm
CC D3 (SNRPD3); such methylation being required for the assembly and
CC biogenesis of snRNP core particles. Specifically mediates the symmetric
CC dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in
CC gene imprinting by being recruited by CTCFL at the H19 imprinted
CC control region (ICR) and methylating histone H4 to form H4R3me2s,
CC possibly leading to recruit DNA methyltransferases at these sites. May
CC also play a role in embryonic stem cell (ESC) pluripotency. Also able
CC to mediate the arginine methylation of histone H2A and myelin basic
CC protein (MBP) in vitro; the relevance of such results is however
CC unclear in vivo. {ECO:0000269|PubMed:15044439,
CC ECO:0000269|PubMed:15494416, ECO:0000269|PubMed:17709427,
CC ECO:0000269|PubMed:19110445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65280; EC=2.1.1.321;
CC Evidence={ECO:0000269|PubMed:25294873};
CC -!- SUBUNIT: Homodimer and heterodimer (By similarity). Interacts with
CC CTCFL (By similarity). Interacts with PRMT5 and SNRPD3. {ECO:0000250,
CC ECO:0000269|PubMed:17709427}.
CC -!- INTERACTION:
CC Q9NVM4; P00966: ASS1; NbExp=9; IntAct=EBI-3215577, EBI-536842;
CC Q9NVM4; P05198: EIF2S1; NbExp=5; IntAct=EBI-3215577, EBI-1056162;
CC Q9NVM4; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-3215577, EBI-10271199;
CC Q9NVM4; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-3215577, EBI-11962468;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15494416}.
CC Nucleus {ECO:0000269|PubMed:15494416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NVM4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVM4-2; Sequence=VSP_005213, VSP_005214;
CC Name=3;
CC IsoId=Q9NVM4-3; Sequence=VSP_037253;
CC Name=4;
CC IsoId=Q9NVM4-4; Sequence=VSP_037254, VSP_037255;
CC -!- DISEASE: Short stature, brachydactyly, impaired intellectual
CC developmental, and seizures (SBIDDS) [MIM:617157]: An autosomal
CC recessive disease characterized by developmental delay, learning
CC disabilities, mild intellectual disability, delayed speech, and
CC skeletal abnormalities. Skeletal features include short stature,
CC brachydactyly, and short metacarpals and metatarsals.
CC {ECO:0000269|PubMed:26437029}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: May be involved in etoposide-induced cytotoxicity, a
CC chemotherapeutic agent frequently used for testicular cancer and small-
CC cell lung cancer that can cause cytotoxicity in the treatment of other
CC cancers. Down-regulation confers increased sensitivity to the Top1
CC inhibitor camptothecin (CPT).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Protein arginine N-methyltransferase family. PRMT7
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14215.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK001502; BAA91726.1; -; mRNA.
DR EMBL; AK022739; BAB14215.1; ALT_INIT; mRNA.
DR EMBL; AK056647; BAG51772.1; -; mRNA.
DR EMBL; AK097175; BAG53431.1; -; mRNA.
DR EMBL; AK304605; BAG65391.1; -; mRNA.
DR EMBL; BC000146; AAH00146.1; -; mRNA.
DR EMBL; AB067520; BAB67826.1; -; mRNA.
DR CCDS; CCDS10866.1; -. [Q9NVM4-1]
DR CCDS; CCDS54033.1; -. [Q9NVM4-3]
DR RefSeq; NP_001171753.1; NM_001184824.1. [Q9NVM4-3]
DR RefSeq; NP_001276947.1; NM_001290018.1. [Q9NVM4-1]
DR RefSeq; NP_061896.1; NM_019023.2. [Q9NVM4-1]
DR RefSeq; XP_016878783.1; XM_017023294.1.
DR RefSeq; XP_016878784.1; XM_017023295.1.
DR AlphaFoldDB; Q9NVM4; -.
DR SMR; Q9NVM4; -.
DR BioGRID; 119992; 41.
DR CORUM; Q9NVM4; -.
DR IntAct; Q9NVM4; 20.
DR MINT; Q9NVM4; -.
DR STRING; 9606.ENSP00000343103; -.
DR BindingDB; Q9NVM4; -.
DR ChEMBL; CHEMBL3562175; -.
DR GuidetoPHARMACOLOGY; 1258; -.
DR GlyGen; Q9NVM4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVM4; -.
DR PhosphoSitePlus; Q9NVM4; -.
DR BioMuta; PRMT7; -.
DR DMDM; 20137529; -.
DR EPD; Q9NVM4; -.
DR jPOST; Q9NVM4; -.
DR MassIVE; Q9NVM4; -.
DR MaxQB; Q9NVM4; -.
DR PaxDb; Q9NVM4; -.
DR PeptideAtlas; Q9NVM4; -.
DR PRIDE; Q9NVM4; -.
DR ProteomicsDB; 82826; -. [Q9NVM4-1]
DR ProteomicsDB; 82827; -. [Q9NVM4-2]
DR ProteomicsDB; 82828; -. [Q9NVM4-3]
DR ProteomicsDB; 82829; -. [Q9NVM4-4]
DR Antibodypedia; 29775; 255 antibodies from 33 providers.
DR DNASU; 54496; -.
DR Ensembl; ENST00000339507.9; ENSP00000343103.5; ENSG00000132600.18. [Q9NVM4-1]
DR Ensembl; ENST00000441236.3; ENSP00000409324.2; ENSG00000132600.18. [Q9NVM4-1]
DR Ensembl; ENST00000449359.7; ENSP00000414716.3; ENSG00000132600.18. [Q9NVM4-3]
DR Ensembl; ENST00000687558.1; ENSP00000509003.1; ENSG00000132600.18. [Q9NVM4-1]
DR Ensembl; ENST00000692760.1; ENSP00000510748.1; ENSG00000132600.18. [Q9NVM4-1]
DR GeneID; 54496; -.
DR KEGG; hsa:54496; -.
DR MANE-Select; ENST00000441236.3; ENSP00000409324.2; NM_019023.5; NP_061896.1.
DR UCSC; uc010vlg.3; human. [Q9NVM4-1]
DR CTD; 54496; -.
DR DisGeNET; 54496; -.
DR GeneCards; PRMT7; -.
DR HGNC; HGNC:25557; PRMT7.
DR HPA; ENSG00000132600; Low tissue specificity.
DR MalaCards; PRMT7; -.
DR MIM; 610087; gene.
DR MIM; 617157; phenotype.
DR neXtProt; NX_Q9NVM4; -.
DR OpenTargets; ENSG00000132600; -.
DR Orphanet; 464288; Short stature-brachydactyly-obesity-global developmental delay syndrome.
DR PharmGKB; PA143485581; -.
DR VEuPathDB; HostDB:ENSG00000132600; -.
DR eggNOG; KOG1501; Eukaryota.
DR GeneTree; ENSGT00940000156879; -.
DR HOGENOM; CLU_015180_0_0_1; -.
DR InParanoid; Q9NVM4; -.
DR OMA; LPMANCA; -.
DR OrthoDB; 408622at2759; -.
DR PhylomeDB; Q9NVM4; -.
DR TreeFam; TF315221; -.
DR BioCyc; MetaCyc:HS05660-MON; -.
DR BRENDA; 2.1.1.321; 2681.
DR PathwayCommons; Q9NVM4; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR SignaLink; Q9NVM4; -.
DR BioGRID-ORCS; 54496; 48 hits in 1101 CRISPR screens.
DR ChiTaRS; PRMT7; human.
DR GenomeRNAi; 54496; -.
DR Pharos; Q9NVM4; Tchem.
DR PRO; PR:Q9NVM4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NVM4; protein.
DR Bgee; ENSG00000132600; Expressed in right hemisphere of cerebellum and 110 other tissues.
DR ExpressionAtlas; Q9NVM4; baseline and differential.
DR Genevisible; Q9NVM4; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016277; F:[myelin basic protein]-arginine N-methyltransferase activity; IDA:HGNC-UCL.
DR GO; GO:0042393; F:histone binding; IC:HGNC-UCL.
DR GO; GO:0044020; F:histone methyltransferase activity (H4-R3 specific); ISS:UniProtKB.
DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IDA:HGNC-UCL.
DR GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:HGNC-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0034969; P:histone arginine methylation; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; IDA:HGNC-UCL.
DR GO; GO:0018216; P:peptidyl-arginine methylation; IDA:HGNC-UCL.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; ISS:UniProtKB.
DR GO; GO:0043393; P:regulation of protein binding; IC:HGNC-UCL.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 2.
DR InterPro; IPR025799; Arg_MeTrfase.
DR InterPro; IPR014644; MeTrfase_PRMT7.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11006; PTHR11006; 1.
DR PIRSF; PIRSF036946; Arg_N-mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
DR PROSITE; PS51678; SAM_MT_PRMT; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Cytoplasm; Differentiation;
KW Disease variant; Dwarfism; Intellectual disability; Methylation;
KW Methyltransferase; Nucleus; Reference proteome; Repeat;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..692
FT /note="Protein arginine N-methyltransferase 7"
FT /id="PRO_0000212335"
FT DOMAIN 14..345
FT /note="SAM-dependent MTase PRMT-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT DOMAIN 358..684
FT /note="SAM-dependent MTase PRMT-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01015"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT ACT_SITE 153
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q922X9"
FT VAR_SEQ 45..94
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037253"
FT VAR_SEQ 95..168
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11572484"
FT /id="VSP_005213"
FT VAR_SEQ 399..472
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11572484"
FT /id="VSP_005214"
FT VAR_SEQ 526..567
FT /note="DLWRIRSPCGDCEGFDVHIMDDMIKRALDFRESREAEPHPLW -> VCREQQ
FT DVPLVLAATLPCVLAGGCGWGCSFLTGPVADPEPLW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037254"
FT VAR_SEQ 568..692
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037255"
FT VARIANT 32
FT /note="R -> T (in SBIDDS; dbSNP:rs149170494)"
FT /evidence="ECO:0000269|PubMed:26437029"
FT /id="VAR_076329"
FT VARIANT 387
FT /note="R -> G (in SBIDDS; dbSNP:rs762515973)"
FT /evidence="ECO:0000269|PubMed:26437029"
FT /id="VAR_076330"
FT VARIANT 494
FT /note="W -> R (in SBIDDS; dbSNP:rs751670999)"
FT /evidence="ECO:0000269|PubMed:26437029"
FT /id="VAR_076331"
FT CONFLICT 218
FT /note="S -> G (in Ref. 1; BAG53431)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="P -> L (in Ref. 1; BAG53431)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="S -> G (in Ref. 1; BAG51772)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="A -> S (in Ref. 1; BAB14215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 692 AA; 78459 MW; 9E0DB9530154231C CRC64;
MKIFCSRANP TTGSVEWLEE DEHYDYHQEI ARSSYADMLH DKDRNVKYYQ GIRAAVSRVK
DRGQKALVLD IGTGTGLLSM MAVTAGADFC YAIEVFKPMA DAAVKIVEKN GFSDKIKVIN
KHSTEVTVGP EGDMPCRANI LVTELFDTEL IGEGALPSYE HAHRHLVEEN CEAVPHRATV
YAQLVESGRM WSWNKLFPIH VQTSLGEQVI VPPVDVESCP GAPSVCDIQL NQVSPADFTV
LSDVLPMFSI DFSKQVSSSA ACHSRRFEPL TSGRAQVVLS WWDIEMDPEG KIKCTMAPFW
AHSDPEEMQW RDHWMQCVYF LPQEEPVVQG SALYLVAHHD DYCVWYSLQR TSPEKNERVR
QMRPVCDCQA HLLWNRPRFG EINDQDRTDR YVQALRTVLK PDSVCLCVSD GSLLSVLAHH
LGVEQVFTVE SSAASHKLLR KIFKANHLED KINIIEKRPE LLTNEDLQGR KVSLLLGEPF
FTTSLLPWHN LYFWYVRTAV DQHLGPGAMV MPQAASLHAV VVEFRDLWRI RSPCGDCEGF
DVHIMDDMIK RALDFRESRE AEPHPLWEYP CRSLSEPWQI LTFDFQQPVP LQPLCAEGTV
ELRRPGQSHA AVLWMEYHLT PECTLSTGLL EPADPEGGCC WNPHCKQAVY FFSPAPDPRA
LLGGPRTVSY AVEFHPDTGD IIMEFRHADT PD
