ID   PLOD2_HUMAN             Reviewed;         737 AA.
AC   O00469; B3KWS3; Q59ED2; Q8N170;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   13-FEB-2019, entry version 176.
DE   RecName: Full=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2;
DE            EC=1.14.11.4 {ECO:0000250|UniProtKB:P24802};
DE   AltName: Full=Lysyl hydroxylase 2;
DE            Short=LH2;
DE   Flags: Precursor;
GN   Name=PLOD2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=9054364; DOI=10.1074/jbc.272.11.6831;
RA   Valtavaara M., Papponen H., Pirttila A.M., Hiltunen K., Helander H.,
RA   Myllylae R.;
RT   "Cloning and characterization of a novel human lysyl hydroxylase
RT   isoform highly expressed in pancreas and muscle.";
RL   J. Biol. Chem. 272:6831-6834(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Esophagus;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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 MRNA] (ISOFORM 1).
RC   TISSUE=Aortic endothelium;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Skin fibroblast;
RX   PubMed=10372558; DOI=10.1016/S0945-053X(99)00013-X;
RA   Yeowell H.N., Walker L.C.;
RT   "Tissue specificity of a new splice form of the human lysyl
RT   hydroxylase 2 gene.";
RL   Matrix Biol. 18:179-187(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320 AND TYR-323, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-209 AND ASN-522.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [9]
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.,
RA   Buerckstuemmer T., 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   [10]
RP   VARIANTS BRKS2 VAL-601 AND ILE-608.
RX   PubMed=12881513; DOI=10.1074/jbc.M307380200;
RA   van der Slot A.J., Zuurmond A.-M., Bardoel A.F.J., Wijmenga C.,
RA   Pruijs H.E.H., Sillence D.O., Brinckmann J., Abraham D.J., Black C.M.,
RA   Verzijl N., DeGroot J., Hanemaaijer R., TeKoppele J.M.,
RA   Huizinga T.W.J., Bank R.A.;
RT   "Identification of PLOD2 as telopeptide lysyl hydroxylase, an
RT   important enzyme in fibrosis.";
RL   J. Biol. Chem. 278:40967-40972(2003).
RN   [11]
RP   VARIANT BRKS2 HIS-598.
RX   PubMed=15523624; DOI=10.1002/ajmg.a.30231;
RA   Ha-Vinh R., Alanay Y., Bank R.A., Campos-Xavier A.B., Zankl A.,
RA   Superti-Furga A., Bonafe L.;
RT   "Phenotypic and molecular characterization of Bruck syndrome
RT   (osteogenesis imperfecta with contractures of the large joints) caused
RT   by a recessive mutation in PLOD2.";
RL   Am. J. Med. Genet. A 131:115-120(2004).
RN   [12]
RP   VARIANT AR-OI CYS-601.
RX   PubMed=22689593; DOI=10.1002/humu.22133;
RA   Puig-Hervas M.T., Temtamy S., Aglan M., Valencia M., Martinez-Glez V.,
RA   Ballesta-Martinez M.J., Lopez-Gonzalez V., Ashour A.M., Amr K.,
RA   Pulido V., Guillen-Navarro E., Lapunzina P., Caparros-Martin J.A.,
RA   Ruiz-Perez V.L.;
RT   "Mutations in PLOD2 cause autosomal-recessive connective tissue
RT   disorders within the Bruck syndrome--osteogenesis imperfecta
RT   phenotypic spectrum.";
RL   Hum. Mutat. 33:1444-1449(2012).
CC   -!- FUNCTION: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences
CC       in collagens. These hydroxylysines serve as sites of attachment
CC       for carbohydrate units and are essential for the stability of the
CC       intermolecular collagen cross-links.
CC       {ECO:0000250|UniProtKB:P24802}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-lysyl-[procollagen] + O2 = (5R)-5-
CC         hydroxy-L-lysyl-[procollagen] + CO2 + succinate;
CC         Xref=Rhea:RHEA:16569, Rhea:RHEA-COMP:12751, Rhea:RHEA-
CC         COMP:12752, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:133442; EC=1.14.11.4;
CC         Evidence={ECO:0000250|UniProtKB:P24802};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:P24802};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000250|UniProtKB:P24802};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P24802}.
CC   -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane;
CC       Peripheral membrane protein; Lumenal side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=A;
CC         IsoId=O00469-1; Sequence=Displayed;
CC       Name=2; Synonyms=B;
CC         IsoId=O00469-2; Sequence=VSP_013467;
CC       Name=3;
CC         IsoId=O00469-3; Sequence=VSP_057221, VSP_057222, VSP_013467;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Highly expressed in pancreas and muscle.
CC       Isoform 1 and isoform 2 are expressed in the majority of the
CC       examined cell types. Isoform 2 is specifically expressed in skin,
CC       lung, dura and aorta. {ECO:0000269|PubMed:10372558}.
CC   -!- DISEASE: Bruck syndrome 2 (BRKS2) [MIM:609220]: An autosomal
CC       recessive disease characterized by generalized osteopenia,
CC       congenital joint contractures, fragile bones with onset of
CC       fractures in infancy or early childhood, short stature, severe
CC       limb deformity, progressive scoliosis, and pterygia. It is
CC       distinguished from osteogenesis imperfecta by the absence of
CC       hearing loss and dentinogenesis imperfecta, and by the presence of
CC       clubfoot and congenital joint limitations.
CC       {ECO:0000269|PubMed:12881513, ECO:0000269|PubMed:15523624}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry. The molecular defect leading to Bruck
CC       syndrome is an aberrant cross-linking of bone collagen, due to
CC       underhydroxylation of lysine residues within the telopeptides of
CC       type I collagen, whereas the lysine residues in the triple helix
CC       are normal.
CC   -!- DISEASE: Note=PLOD2 mutations give rise to a broad variety of
CC       phenotypes with variable degrees of severity of bone fragility and
CC       joint contractures. Disease-associated mutations have been found
CC       in patients with autosomal recessive osteogenesis imperfecta (AR-
CC       OI) (PubMed:22689593). {ECO:0000269|PubMed:22689593}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD93116.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database;
CC       Note=Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (PLOD2);
CC       URL="http://oi.gene.le.ac.uk/home.php?select_db=PLOD2";
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DR   EMBL; U84573; AAB58363.1; -; mRNA.
DR   EMBL; AK125700; BAG54235.1; -; mRNA.
DR   EMBL; AB209879; BAD93116.1; ALT_INIT; mRNA.
DR   EMBL; AC092982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC037169; AAH37169.1; -; mRNA.
DR   CCDS; CCDS3131.1; -. [O00469-1]
DR   CCDS; CCDS3132.1; -. [O00469-2]
DR   PIR; A59144; A59144.
DR   RefSeq; NP_000926.2; NM_000935.2. [O00469-1]
DR   RefSeq; NP_891988.1; NM_182943.2. [O00469-2]
DR   UniGene; Hs.477866; -.
DR   ProteinModelPortal; O00469; -.
DR   SMR; O00469; -.
DR   BioGrid; 111367; 51.
DR   CORUM; O00469; -.
DR   IntAct; O00469; 15.
DR   MINT; O00469; -.
DR   STRING; 9606.ENSP00000282903; -.
DR   DrugBank; DB00126; Vitamin C.
DR   GlyConnect; 746; -.
DR   iPTMnet; O00469; -.
DR   PhosphoSitePlus; O00469; -.
DR   SwissPalm; O00469; -.
DR   UniCarbKB; O00469; -.
DR   BioMuta; PLOD2; -.
DR   EPD; O00469; -.
DR   jPOST; O00469; -.
DR   MaxQB; O00469; -.
DR   PaxDb; O00469; -.
DR   PeptideAtlas; O00469; -.
DR   PRIDE; O00469; -.
DR   ProteomicsDB; 47915; -.
DR   ProteomicsDB; 47916; -. [O00469-2]
DR   Ensembl; ENST00000282903; ENSP00000282903; ENSG00000152952. [O00469-2]
DR   Ensembl; ENST00000360060; ENSP00000353170; ENSG00000152952. [O00469-1]
DR   Ensembl; ENST00000461497; ENSP00000419354; ENSG00000152952. [O00469-3]
DR   GeneID; 5352; -.
DR   KEGG; hsa:5352; -.
DR   UCSC; uc003evq.2; human. [O00469-1]
DR   CTD; 5352; -.
DR   DisGeNET; 5352; -.
DR   EuPathDB; HostDB:ENSG00000152952.11; -.
DR   GeneCards; PLOD2; -.
DR   HGNC; HGNC:9082; PLOD2.
DR   HPA; CAB025898; -.
DR   HPA; HPA069126; -.
DR   MalaCards; PLOD2; -.
DR   MIM; 601865; gene.
DR   MIM; 609220; phenotype.
DR   neXtProt; NX_O00469; -.
DR   OpenTargets; ENSG00000152952; -.
DR   Orphanet; 2771; Bruck syndrome.
DR   PharmGKB; PA33412; -.
DR   eggNOG; KOG1971; Eukaryota.
DR   eggNOG; ENOG410Y4QU; LUCA.
DR   GeneTree; ENSGT00940000159216; -.
DR   HOGENOM; HOG000231099; -.
DR   HOVERGEN; HBG053618; -.
DR   InParanoid; O00469; -.
DR   KO; K13645; -.
DR   OMA; GVWNIPY; -.
DR   OrthoDB; 194164at2759; -.
DR   PhylomeDB; O00469; -.
DR   TreeFam; TF313826; -.
DR   BRENDA; 1.14.11.4; 2681.
DR   Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR   ChiTaRS; PLOD2; human.
DR   GenomeRNAi; 5352; -.
DR   PRO; PR:O00469; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000152952; Expressed in 223 organ(s), highest expression level in tibia.
DR   ExpressionAtlas; O00469; baseline and differential.
DR   Genevisible; O00469; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; 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:0008475; F:procollagen-lysine 5-dioxygenase activity; IDA:CAFA.
DR   GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
DR   GO; GO:0030199; P:collagen fibril organization; IBA:GO_Central.
DR   GO; GO:0032963; P:collagen metabolic process; IBA:GO_Central.
DR   GO; GO:0046947; P:hydroxylysine biosynthetic process; IDA:CAFA.
DR   GO; GO:0017185; P:peptidyl-lysine hydroxylation; IDA:CAFA.
DR   GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR001006; Procol_lys_dOase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   PROSITE; PS01325; LYS_HYDROXYLASE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Dioxygenase;
KW   Disease mutation; Endoplasmic reticulum; Glycoprotein; Iron; Membrane;
KW   Metal-binding; Osteogenesis imperfecta; Oxidoreductase;
KW   Phosphoprotein; Reference proteome; Signal; Vitamin C.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    737       Procollagen-lysine,2-oxoglutarate 5-
FT                                dioxygenase 2.
FT                                /FTId=PRO_0000024683.
FT   DOMAIN      644    737       Fe2OG dioxygenase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   ACT_SITE    728    728       {ECO:0000255}.
FT   METAL       666    666       Iron. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   METAL       668    668       Iron. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   METAL       718    718       Iron. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00805}.
FT   MOD_RES     320    320       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18088087}.
FT   MOD_RES     323    323       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:18088087}.
FT   MOD_RES     704    704       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q9R0B9}.
FT   CARBOHYD     63     63       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    209    209       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    297    297       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    365    365       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    522    522       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    696    696       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    725    725       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ       1     36       MGGCTVKPQLLLLALVLHPWNPCLGADSEKPSSIPT -> M
FT                                LENHILHKRIYILTFFSQQIFILCHAHFIFFFTVR (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057221.
FT   VAR_SEQ      37    376       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_057222.
FT   VAR_SEQ     500    500       M -> MTLQREKDSPTPETFQMLSPPK (in isoform 2
FT                                and isoform 3).
FT                                {ECO:0000303|PubMed:10372558,
FT                                ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_013467.
FT   VARIANT     598    598       R -> H (in BRKS2; dbSNP:rs121434461).
FT                                {ECO:0000269|PubMed:15523624}.
FT                                /FTId=VAR_022164.
FT   VARIANT     601    601       G -> C (in AR-OI; probable disease-
FT                                associated mutation found in patients
FT                                with osteogenesis imperfecta;
FT                                dbSNP:rs762788421).
FT                                {ECO:0000269|PubMed:22689593}.
FT                                /FTId=VAR_069531.
FT   VARIANT     601    601       G -> V (in BRKS2; dbSNP:rs121434460).
FT                                {ECO:0000269|PubMed:12881513}.
FT                                /FTId=VAR_022165.
FT   VARIANT     608    608       T -> I (in BRKS2; dbSNP:rs121434459).
FT                                {ECO:0000269|PubMed:12881513}.
FT                                /FTId=VAR_022166.
FT   CONFLICT    624    624       H -> D (in Ref. 1; AAB58363).
FT                                {ECO:0000305}.
SQ   SEQUENCE   737 AA;  84686 MW;  C9AEA79A574D6B66 CRC64;
     MGGCTVKPQL LLLALVLHPW NPCLGADSEK PSSIPTDKLL VITVATKESD GFHRFMQSAK
     YFNYTVKVLG QGEEWRGGDG INSIGGGQKV RLMKEVMEHY ADQDDLVVMF TECFDVIFAG
     GPEEVLKKFQ KANHKVVFAA DGILWPDKRL ADKYPVVHIG KRYLNSGGFI GYAPYVNRIV
     QQWNLQDNDD DQLFYTKVYI DPLKREAINI TLDHKCKIFQ TLNGAVDEVV LKFENGKARA
     KNTFYETLPV AINGNGPTKI LLNYFGNYVP NSWTQDNGCT LCEFDTVDLS AVDVHPNVSI
     GVFIEQPTPF LPRFLDILLT LDYPKEALKL FIHNKEVYHE KDIKVFFDKA KHEIKTIKIV
     GPEENLSQAE ARNMGMDFCR QDEKCDYYFS VDADVVLTNP RTLKILIEQN RKIIAPLVTR
     HGKLWSNFWG ALSPDGYYAR SEDYVDIVQG NRVGVWNVPY MANVYLIKGK TLRSEMNERN
     YFVRDKLDPD MALCRNAREM GVFMYISNRH EFGRLLSTAN YNTSHYNNDL WQIFENPVDW
     KEKYINRDYS KIFTENIVEQ PCPDVFWFPI FSEKACDELV EEMEHYGKWS GGKHHDSRIS
     GGYENVPTDD IHMKQVDLEN VWLHFIREFI APVTLKVFAG YYTKGFALLN FVVKYSPERQ
     RSLRPHHDAS TFTINIALNN VGEDFQGGGC KFLRYNCSIE SPRKGWSFMH PGRLTHLHEG
     LPVKNGTRYI AVSFIDP
//