P3H2_HUMAN
ID P3H2_HUMAN Reviewed; 708 AA.
AC Q8IVL5; B3KPK0; B3KWI9; D3DNV8; Q9NVI2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Prolyl 3-hydroxylase 2 {ECO:0000312|HGNC:HGNC:19317};
DE EC=1.14.11.7 {ECO:0000269|PubMed:18487197};
DE AltName: Full=Leprecan-like protein 1 {ECO:0000303|PubMed:15063763};
DE AltName: Full=Myxoid liposarcoma-associated protein 4 {ECO:0000303|PubMed:10449603};
DE Flags: Precursor;
GN Name=P3H2 {ECO:0000312|HGNC:HGNC:19317};
GN Synonyms=LEPREL1 {ECO:0000303|PubMed:15063763},
GN MLAT4 {ECO:0000303|PubMed:10449603};
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).
RC TISSUE=Liposarcoma;
RX PubMed=10449603;
RX DOI=10.1002/(sici)1097-0215(19990924)83:1<30::aid-ijc6>3.0.co;2-4;
RA Thelin-Jaernum S., Lassen C., Panagopoulos I., Mandahl N., Aaman P.;
RT "Identification of genes differentially expressed in TLS-CHOP carrying
RT myxoid liposarcomas.";
RL Int. J. Cancer 83:30-33(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND POSSIBLE FUNCTION.
RC TISSUE=Liposarcoma;
RX PubMed=15063763; DOI=10.1016/j.bbrc.2004.03.060;
RA Jaernum S., Kjellman C., Darabi A., Nilsson I., Edvardsen K., Aaman P.;
RT "LEPREL1, a novel ER and Golgi resident member of the Leprecan family.";
RL Biochem. Biophys. Res. Commun. 317:342-351(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Teratocarcinoma, and Tongue;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-708 (ISOFORM 1).
RC TISSUE=Lung;
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=18487197; DOI=10.1074/jbc.m802973200;
RA Tiainen P., Pasanen A., Sormunen R., Myllyharju J.;
RT "Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an
RT enzyme modifying the basement membrane collagen IV.";
RL J. Biol. Chem. 283:19432-19439(2008).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-613.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [9]
RP VARIANT MCVD VAL-508, AND CHARACTERIZATION OF VARIANT MCVD VAL-508.
RX PubMed=21885030; DOI=10.1016/j.ajhg.2011.08.003;
RA Mordechai S., Gradstein L., Pasanen A., Ofir R., El Amour K., Levy J.,
RA Belfair N., Lifshitz T., Joshua S., Narkis G., Elbedour K., Myllyharju J.,
RA Birk O.S.;
RT "High myopia caused by a mutation in LEPREL1, encoding prolyl 3-hydroxylase
RT 2.";
RL Am. J. Hum. Genet. 89:438-445(2011).
CC -!- FUNCTION: Prolyl 3-hydroxylase that catalyzes the post-translational
CC formation of 3-hydroxyproline on collagens (PubMed:18487197).
CC Contributes to proline 3-hydroxylation of collagen COL4A1 and COL1A1 in
CC tendons, the eye sclera and in the eye lens capsule (By similarity).
CC Has high activity with the type IV collagen COL4A1, and lower activity
CC with COL1A1 (PubMed:18487197). Catalyzes hydroxylation of the first Pro
CC in Gly-Pro-Hyp sequences where Hyp is 4-hydroxyproline
CC (PubMed:18487197). Has no activity on substrates that lack 4-
CC hydroxyproline in the third position (PubMed:18487197).
CC {ECO:0000250|UniProtKB:Q8CG71, ECO:0000269|PubMed:18487197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC trans-3-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:22872, Rhea:RHEA-
CC COMP:11676, Rhea:RHEA-COMP:11678, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:85428; EC=1.14.11.7;
CC Evidence={ECO:0000269|PubMed:18487197};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000305|PubMed:18487197};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000305|PubMed:18487197};
CC -!- ACTIVITY REGULATION: Inhibited by pyridine 2,4-dicarboxylate, an analog
CC of 2-oxoglutarate. {ECO:0000269|PubMed:18487197}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for 2-oxoglutarate {ECO:0000269|PubMed:18487197};
CC KM=110 uM for ascorbate {ECO:0000269|PubMed:18487197};
CC KM=0.5 uM for Fe(2+) {ECO:0000269|PubMed:18487197};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:15063763}. Sarcoplasmic reticulum
CC {ECO:0000305|PubMed:15063763}. Golgi apparatus
CC {ECO:0000269|PubMed:15063763}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IVL5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IVL5-2; Sequence=VSP_053814;
CC -!- TISSUE SPECIFICITY: Expression localized to the epithelia of bile ducts
CC and to the sacroplasm of heart muscle and skeletal muscle. In the
CC pancreas, localized to a subpopulation of Langerhans islet cells and in
CC the salivary gland, expressed in acinar cells (at protein level)
CC (PubMed:15063763). Expressed in adult heart, placenta, lung, liver,
CC skeletal muscle and kidney (PubMed:15063763, PubMed:18487197). Detected
CC in fetal heart, spleen, lung, liver skeletal muscle and kidney
CC (PubMed:18487197). {ECO:0000269|PubMed:15063763,
CC ECO:0000269|PubMed:18487197}.
CC -!- DISEASE: Myopia, high, with cataract and vitreoretinal degeneration
CC (MCVD) [MIM:614292]: A disorder characterized by severe myopia with
CC variable expressivity of cataract and vitreoretinal degeneration. Some
CC patients manifest lens subluxation, lens instability and retinal
CC detachment. {ECO:0000269|PubMed:21885030}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the leprecan family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91769.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ430351; CAD23039.2; -; mRNA.
DR EMBL; AK001580; BAA91769.1; ALT_INIT; mRNA.
DR EMBL; AK056447; BAG51712.1; -; mRNA.
DR EMBL; AK125134; BAG54151.1; -; mRNA.
DR EMBL; AC016966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC063939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099660; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78109.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78110.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78111.1; -; Genomic_DNA.
DR EMBL; BC005029; AAH05029.1; -; mRNA.
DR CCDS; CCDS3294.1; -. [Q8IVL5-1]
DR CCDS; CCDS46981.1; -. [Q8IVL5-2]
DR RefSeq; NP_001127890.1; NM_001134418.1. [Q8IVL5-2]
DR RefSeq; NP_060662.2; NM_018192.3. [Q8IVL5-1]
DR RefSeq; XP_011511257.1; XM_011512955.1. [Q8IVL5-2]
DR AlphaFoldDB; Q8IVL5; -.
DR SMR; Q8IVL5; -.
DR BioGRID; 120510; 25.
DR IntAct; Q8IVL5; 16.
DR STRING; 9606.ENSP00000316881; -.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugBank; DB00172; Proline.
DR DrugBank; DB00139; Succinic acid.
DR GlyGen; Q8IVL5; 2 sites.
DR iPTMnet; Q8IVL5; -.
DR PhosphoSitePlus; Q8IVL5; -.
DR BioMuta; P3H2; -.
DR DMDM; 74714365; -.
DR EPD; Q8IVL5; -.
DR jPOST; Q8IVL5; -.
DR MassIVE; Q8IVL5; -.
DR MaxQB; Q8IVL5; -.
DR PaxDb; Q8IVL5; -.
DR PeptideAtlas; Q8IVL5; -.
DR PRIDE; Q8IVL5; -.
DR ProteomicsDB; 12740; -.
DR ProteomicsDB; 70737; -. [Q8IVL5-1]
DR Antibodypedia; 1998; 118 antibodies from 20 providers.
DR DNASU; 55214; -.
DR Ensembl; ENST00000319332.10; ENSP00000316881.5; ENSG00000090530.10. [Q8IVL5-1]
DR Ensembl; ENST00000427335.6; ENSP00000408947.2; ENSG00000090530.10. [Q8IVL5-2]
DR GeneID; 55214; -.
DR KEGG; hsa:55214; -.
DR MANE-Select; ENST00000319332.10; ENSP00000316881.5; NM_018192.4; NP_060662.2.
DR UCSC; uc003fsg.4; human. [Q8IVL5-1]
DR CTD; 55214; -.
DR DisGeNET; 55214; -.
DR GeneCards; P3H2; -.
DR HGNC; HGNC:19317; P3H2.
DR HPA; ENSG00000090530; Low tissue specificity.
DR MalaCards; P3H2; -.
DR MIM; 610341; gene.
DR MIM; 614292; phenotype.
DR neXtProt; NX_Q8IVL5; -.
DR OpenTargets; ENSG00000090530; -.
DR Orphanet; 98619; Rare isolated myopia.
DR PharmGKB; PA134922807; -.
DR VEuPathDB; HostDB:ENSG00000090530; -.
DR eggNOG; KOG4459; Eukaryota.
DR GeneTree; ENSGT00940000159593; -.
DR HOGENOM; CLU_017820_0_0_1; -.
DR InParanoid; Q8IVL5; -.
DR OMA; AKPHMED; -.
DR OrthoDB; 660619at2759; -.
DR PhylomeDB; Q8IVL5; -.
DR TreeFam; TF320837; -.
DR BRENDA; 1.14.11.7; 2681.
DR PathwayCommons; Q8IVL5; -.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR SignaLink; Q8IVL5; -.
DR BioGRID-ORCS; 55214; 5 hits in 1067 CRISPR screens.
DR ChiTaRS; P3H2; human.
DR GenomeRNAi; 55214; -.
DR Pharos; Q8IVL5; Tbio.
DR PRO; PR:Q8IVL5; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8IVL5; protein.
DR Bgee; ENSG00000090530; Expressed in adrenal tissue and 136 other tissues.
DR ExpressionAtlas; Q8IVL5; baseline and differential.
DR Genevisible; Q8IVL5; HS.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0032963; P:collagen metabolic process; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0019511; P:peptidyl-proline hydroxylation; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR039575; P3H.
DR InterPro; IPR039838; P3H2.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR14049; PTHR14049; 1.
DR PANTHER; PTHR14049:SF1; PTHR14049:SF1; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Dioxygenase; Disease variant; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; Sarcoplasmic reticulum; Signal; TPR repeat;
KW Vitamin C.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..708
FT /note="Prolyl 3-hydroxylase 2"
FT /id="PRO_0000240356"
FT REPEAT 44..77
FT /note="TPR 1"
FT REPEAT 148..181
FT /note="TPR 2"
FT REPEAT 210..243
FT /note="TPR 3"
FT REPEAT 306..339
FT /note="TPR 4"
FT DOMAIN 557..671
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MOTIF 705..708
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 662
FT /evidence="ECO:0000250"
FT BINDING 580
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 582
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 652
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..181
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053814"
FT VARIANT 508
FT /note="G -> V (in MCVD; loss of function;
FT dbSNP:rs724159988)"
FT /evidence="ECO:0000269|PubMed:21885030"
FT /id="VAR_066637"
FT VARIANT 613
FT /note="D -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036123"
FT CONFLICT 477
FT /note="R -> Q (in Ref. 3; BAG51712)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 80984 MW; B9E680C90D607291 CRC64;
MRERIWAPPL LLLLPLLLPP PLWGGPPDSP RRELELEPGP LQPFDLLYAS GAAAYYSGDY
ERAVRDLEAA LRSHRRLREI RTRCARHCAA RHPLPPPPPG EGPGAELPLF RSLLGRARCY
RSCETQRLGG PASRHRVSED VRSDFQRRVP YNYLQRAYIK LNQLEKAVEA AHTFFVANPE
HMEMQQNIEN YRATAGVEAL QLVDREAKPH MESYNAGVKH YEADDFEMAI RHFEQALREY
FVEDTECRTL CEGPQRFEEY EYLGYKAGLY EAIADHYMQV LVCQHECVRE LATRPGRLSP
IENFLPLHYD YLQFAYYRVG EYVKALECAK AYLLCHPDDE DVLDNVDYYE SLLDDSIDPA
SIEAREDLTM FVKRHKLESE LIKSAAEGLG FSYTEPNYWI RYGGRQDENR VPSGVNVEGA
EVHGFSMGKK LSPKIDRDLR EGGPLLYENI TFVYNSEQLN GTQRVLLDNV LSEEQCRELH
SVASGIMLVG DGYRGKTSPH TPNEKFEGAT VLKALKSGYE GRVPLKSARL FYDISEKARR
IVESYFMLNS TLYFSYTHMV CRTALSGQQD RRNDLSHPIH ADNCLLDPEA NECWKEPPAY
TFRDYSALLY MNDDFEGGEF IFTEMDAKTV TASIKPKCGR MISFSSGGEN PHGVKAVTKG
KRCAVALWFT LDPLYRELER IQADEVIAIL DQEQQGKHEL NINPKDEL
