PLCH1_HUMAN
ID PLCH1_HUMAN Reviewed; 1693 AA.
AC Q4KWH8; Q29RV9; Q4KWH9; Q68CN0; Q86XK4; Q9H9U2; Q9UPT3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1 {ECO:0000305};
DE EC=3.1.4.11;
DE AltName: Full=Phosphoinositide phospholipase C-eta-1;
DE AltName: Full=Phospholipase C-eta-1;
DE Short=PLC-eta-1;
DE AltName: Full=Phospholipase C-like protein 3;
DE Short=PLC-L3;
GN Name=PLCH1 {ECO:0000312|HGNC:HGNC:29185}; Synonyms=KIAA1069, PLCL3;
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 1 AND 3), FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=15702972; DOI=10.1042/bj20041677;
RA Hwang J.-I., Oh Y.-S., Shin K.-J., Kim H., Ryu S.H., Suh P.-G.;
RT "Molecular cloning and characterization of a novel phospholipase C, PLC-
RT eta.";
RL Biochem. J. 389:181-186(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 926-1693 (ISOFORM 1).
RC TISSUE=Eye, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 216-1693 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-1034 (ISOFORM 4).
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] OF 1470-1693 (ISOFORMS 1/2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by calcium-activated phosphatidylinositol-specific phospholipase C
CC enzymes. {ECO:0000269|PubMed:15702972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000269|PubMed:15702972};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:15702972};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15702972}. Membrane
CC {ECO:0000269|PubMed:15702972}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=PLC-eta-1;
CC IsoId=Q4KWH8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4KWH8-2; Sequence=VSP_032901, VSP_032902;
CC Name=3; Synonyms=PLC-eta-1a;
CC IsoId=Q4KWH8-3; Sequence=VSP_032904, VSP_032905;
CC Name=4;
CC IsoId=Q4KWH8-4; Sequence=VSP_032902, VSP_032903, VSP_032906;
CC -!- TISSUE SPECIFICITY: Expressed in brain and to a lower extent in lung.
CC In brain, it is found in cerebrum, cerebellum and spinal cord.
CC {ECO:0000269|PubMed:15702972}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14129.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY691170; AAW22607.1; -; mRNA.
DR EMBL; AY691171; AAW22608.1; -; mRNA.
DR EMBL; BC043248; AAH43248.2; -; mRNA.
DR EMBL; BC113950; AAI13951.1; -; mRNA.
DR EMBL; AB028992; BAA83021.1; -; mRNA.
DR EMBL; AK022610; BAB14129.1; ALT_INIT; mRNA.
DR EMBL; CR749869; CAH18710.1; -; mRNA.
DR CCDS; CCDS46939.1; -. [Q4KWH8-1]
DR CCDS; CCDS46940.1; -. [Q4KWH8-3]
DR RefSeq; NP_001124432.1; NM_001130960.1. [Q4KWH8-1]
DR RefSeq; NP_001124433.1; NM_001130961.1. [Q4KWH8-3]
DR RefSeq; NP_055811.1; NM_014996.2.
DR RefSeq; XP_016861418.1; XM_017005929.1.
DR AlphaFoldDB; Q4KWH8; -.
DR SMR; Q4KWH8; -.
DR BioGRID; 116651; 49.
DR IntAct; Q4KWH8; 22.
DR MINT; Q4KWH8; -.
DR STRING; 9606.ENSP00000345988; -.
DR SwissLipids; SLP:000000940; -.
DR CarbonylDB; Q4KWH8; -.
DR GlyGen; Q4KWH8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q4KWH8; -.
DR PhosphoSitePlus; Q4KWH8; -.
DR BioMuta; PLCH1; -.
DR DMDM; 121947010; -.
DR EPD; Q4KWH8; -.
DR jPOST; Q4KWH8; -.
DR MassIVE; Q4KWH8; -.
DR MaxQB; Q4KWH8; -.
DR PaxDb; Q4KWH8; -.
DR PeptideAtlas; Q4KWH8; -.
DR PRIDE; Q4KWH8; -.
DR ProteomicsDB; 62214; -. [Q4KWH8-1]
DR ProteomicsDB; 62215; -. [Q4KWH8-2]
DR ProteomicsDB; 62216; -. [Q4KWH8-3]
DR ProteomicsDB; 62217; -. [Q4KWH8-4]
DR Antibodypedia; 46750; 83 antibodies from 23 providers.
DR DNASU; 23007; -.
DR Ensembl; ENST00000334686.6; ENSP00000335469.6; ENSG00000114805.18. [Q4KWH8-2]
DR Ensembl; ENST00000340059.11; ENSP00000345988.7; ENSG00000114805.18. [Q4KWH8-1]
DR Ensembl; ENST00000447496.6; ENSP00000402759.2; ENSG00000114805.18. [Q4KWH8-3]
DR Ensembl; ENST00000494598.5; ENSP00000419100.1; ENSG00000114805.18. [Q4KWH8-4]
DR GeneID; 23007; -.
DR KEGG; hsa:23007; -.
DR UCSC; uc062pff.1; human. [Q4KWH8-1]
DR CTD; 23007; -.
DR DisGeNET; 23007; -.
DR GeneCards; PLCH1; -.
DR HGNC; HGNC:29185; PLCH1.
DR HPA; ENSG00000114805; Tissue enhanced (lymphoid tissue, retina).
DR MIM; 612835; gene.
DR neXtProt; NX_Q4KWH8; -.
DR OpenTargets; ENSG00000114805; -.
DR PharmGKB; PA128394595; -.
DR VEuPathDB; HostDB:ENSG00000114805; -.
DR eggNOG; KOG0169; Eukaryota.
DR GeneTree; ENSGT00940000157185; -.
DR HOGENOM; CLU_002738_0_1_1; -.
DR InParanoid; Q4KWH8; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q4KWH8; -.
DR TreeFam; TF313216; -.
DR BRENDA; 3.1.4.11; 2681.
DR PathwayCommons; Q4KWH8; -.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SignaLink; Q4KWH8; -.
DR BioGRID-ORCS; 23007; 10 hits in 1079 CRISPR screens.
DR ChiTaRS; PLCH1; human.
DR GenomeRNAi; 23007; -.
DR Pharos; Q4KWH8; Tbio.
DR PRO; PR:Q4KWH8; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q4KWH8; protein.
DR Bgee; ENSG00000114805; Expressed in bronchial epithelial cell and 132 other tissues.
DR ExpressionAtlas; Q4KWH8; baseline and differential.
DR Genevisible; Q4KWH8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050429; F:calcium-dependent phospholipase C activity; IDA:MGI.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR028392; PLC-eta1.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF51; PTHR10336:SF51; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transducer.
FT CHAIN 1..1693
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase eta-1"
FT /id="PRO_0000329007"
FT DOMAIN 20..128
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 142..177
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 178..214
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 226..246
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 299..444
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 601..714
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 715..843
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 526..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1300..1316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 442
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 627
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 654
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 758
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 760
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 784
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 813
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 814
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 815
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032901"
FT VAR_SEQ 862..881
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032902"
FT VAR_SEQ 1000..1034
FT /note="AEDKDGRRKGKASIKDPHFLNFNKKLSSSSSALLH -> DSSFCRPTEQAKA
FT EMCKVPFPRQLECVMKMEISET (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032903"
FT VAR_SEQ 1000..1002
FT /note="AED -> VQI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:15702972"
FT /id="VSP_032904"
FT VAR_SEQ 1003..1693
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10470851,
FT ECO:0000303|PubMed:15702972"
FT /id="VSP_032905"
FT VAR_SEQ 1035..1693
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032906"
SQ SEQUENCE 1693 AA; 189223 MW; 00F2ADD21C4D14E6 CRC64;
MADLEVYKNL SPEKVERCMS VMQSGTQMIK LKRGTKGLVR LFYLDEHRTR LRWRPSRKSE
KAKILIDSIY KVTEGRQSEI FHRQAEGNFD PSCCFTIYHG NHMESLDLIT SNPEEARTWI
TGLKYLMAGI SDEDSLAKRQ RTHDQWVKQT FEEADKNGDG LLNIEEIHQL MHKLNVNLPR
RKVRQMFQEA DTDENQGTLT FEEFCVFYKM MSLRRDLYLL LLSYSDKKDH LTVEELAQFL
KVEQKMNNVT TDYCLDIIKK FEVSEENKVK NVLGIEGFTN FMRSPACDIF NPLHHEVYQD
MDQPLCNYYI ASSHNTYLTG DQLLSQSKVD MYARVLQEGC RCVEVDCWDG PDGEPVVHHG
YTLTSKILFR DVVETINKHA FVKNEFPVIL SIENHCSIQQ QRKIAQYLKG IFGDKLDLSS
VDTGECKQLP SPQSLKGKIL VKGKKLPYHL GDDAEEGEVS DEDSADEIED ECKFKLHYSN
GTTEHQVESF IRKKLESLLK ESQIRDKEDP DSFTVRALLK ATHEGLNAHL KQSPDVKESG
KKSHGRSLMT NFGKHKKTTK SRSKSYSTDD EEDTQQSTGK EGGQLYRLGR RRKTMKLCRE
LSDLVVYTNS VAAQDIVDDG TTGNVLSFSE TRAHQVVQQK SEQFMIYNQK QLTRIYPSAY
RIDSSNFNPL PYWNAGCQLV ALNYQSEGRM MQLNRAKFKA NGNCGYVLKP QQMCKGTFNP
FSGDPLPANP KKQLILKVIS GQQLPKPPDS MFGDRGEIID PFVEVEIIGL PVDCCKDQTR
VVDDNGFNPV WEETLTFTVH MPEIALVRFL VWDHDPIGRD FVGQRTVTFS SLVPGYRHVY
LEGLTEASIF VHITINEIYG KWSPLILNPS YTILHFLGAT KNRQLQGLKG LFNKNPRHSS
SENNSHYVRK RSIGDRILRR TASAPAKGRK KSKMGFQEMV EIKDSVSEAT RDQDGVLRRT
TRSLQARPVS MPVDRNLLGA LSLPVSETAK DIEGKENSLA EDKDGRRKGK ASIKDPHFLN
FNKKLSSSSS ALLHKDTSQG DTIVSTAHMS VTGEQLGMSS PRGGRTTSNA TSNCQENPCP
SKSLSPKQHL APDPVVNPTQ DLHGVKIKEK GNPEDFVEGK SILSGSVLSH SNLEIKNLEG
NRGKGRAATS FSLSDVSMLC SDIPDLHSTA ILQESVISHL IDNVTLTNEN EPGSSISALI
GQFDETNNQA LTVVSHLHNT SVMSGHCPLP SLGLKMPIKH GFCKGKSKSS FLCSSPELIA
LSSSETTKHA TNTVYETTCT PISKTKPDDD LSSKAKTAAL ESNLPGSPNT SRGWLPKSPT
KGEDWETLKS CSPASSPDLT LEDVIADPTL CFNSGESSLV EIDGESENLS LTTCEYRREG
TSQLASPLKL KYNQGVVEHF QRGLRNGYCK ETLRPSVPEI FNNIQDVKTQ SISYLAYQGA
GFVHNHFSDS DAKMFQTCVP QQSSAQDMHV PVPKQLAHLP LPALKLPSPC KSKSLGDLTS
EDIACNFESK YQCISKSFVT TGIRDKKGVT VKTKSLEPID ALTEQLRKLV SFDQEDNCQV
LYSKQDANQL PRALVRKLSS RSQSRVRNIA SRAKEKQEAN KQKVPNPSNG AGVVLRNKPS
APTPAVNRHS TGSYIAGYLK NTKGGGLEGR GIPEGACTAL HYGHVDQFCS DNSVLQTEPS
SDDKPEIYFL LRL
