ID   JAG2_HUMAN              Reviewed;        1238 AA.
AC   Q9Y219; Q9UE17; Q9UE99; Q9UNK8; Q9Y6P9; Q9Y6Q0;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Protein jagged-2;
DE            Short=Jagged2;
DE            Short=hJ2;
DE   Flags: Precursor;
GN   Name=JAG2;
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 LONG), AND VARIANT LYS-501.
RX   PubMed=9315665; DOI=10.1128/mcb.17.10.6057;
RA   Luo B., Aster J.C., Hasserjian R.P., Kuo F., Sklar J.;
RT   "Isolation and functional analysis of a cDNA for human Jagged2, a gene
RT   encoding a ligand for the Notch1 receptor.";
RL   Mol. Cell. Biol. 17:6057-6067(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT LYS-501.
RC   TISSUE=Fetal brain;
RX   PubMed=10079256; DOI=10.1016/s0002-9440(10)65325-4;
RA   Gray G.E., Mann R.S., Mitsiadis E., Henrique D., Carcangiu M.-L., Banks A.,
RA   Leiman J., Ward D., Ish-Horowitz D., Artavanis-Tsakonas S.;
RT   "Human ligands of the Notch receptor.";
RL   Am. J. Pathol. 154:785-794(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT), AND
RP   VARIANT LYS-501.
RC   TISSUE=Bone marrow;
RX   PubMed=10662552; DOI=10.1006/geno.1999.6045;
RA   Deng Y., Madan A., Banta A.B., Friedman C., Trask B.J., Hood L., Li L.;
RT   "Characterization, chromosomal localization, and the complete 30-kb DNA
RT   sequence of the human Jagged2 (JAG2) gene.";
RL   Genomics 63:133-138(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-1238 (ISOFORM LONG).
RC   TISSUE=Heart;
RX   PubMed=9486542; DOI=10.1016/s0925-4773(97)00146-9;
RA   Valsecchi C., Ghezzi C., Ballabio A., Rugarli E.I.;
RT   "JAGGED2: a putative Notch ligand expressed in the apical ectodermal ridge
RT   and in sites of epithelial-mesenchymal interactions.";
RL   Mech. Dev. 69:203-207(1997).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND IDENTIFICATION BY
RP   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   [6]
RP   VARIANTS LGMDR27 SER-74; ALA-95; LYS-164; 165-ARG--GLU-1238 DEL; ASP-243;
RP   ILE-358; SER-682; ASP-702 DEL; CYS-712; CYS-825; ARG-839 AND SER-977, AND
RP   INVOLVEMENT IN LGMDR27.
RX   PubMed=33861953; DOI=10.1016/j.ajhg.2021.03.020;
RA   Coppens S., Barnard A.M., Puusepp S., Pajusalu S., Ounap K.,
RA   Vargas-Franco D., Bruels C.C., Donkervoort S., Pais L., Chao K.R.,
RA   Goodrich J.K., England E.M., Weisburd B., Ganesh V.S., Gudmundsson S.,
RA   O'Donnell-Luria A., Nigul M., Ilves P., Mohassel P., Siddique T.,
RA   Milone M., Nicolau S., Maroofian R., Houlden H., Hanna M.G., Quinlivan R.,
RA   Beiraghi Toosi M., Ghayoor Karimiani E., Costagliola S., Deconinck N.,
RA   Kadhim H., Macke E., Lanpher B.C., Klee E.W., Lusakowska A.,
RA   Kostera-Pruszczyk A., Hahn A., Schrank B., Nishino I., Ogasawara M.,
RA   El Sherif R., Stojkovic T., Nelson I., Bonne G., Cohen E., Boland-Auge A.,
RA   Deleuze J.F., Meng Y., Toepf A., Vilain C., Pacak C.A.,
RA   Rivera-Zengotita M.L., Boennemann C.G., Straub V., Handford P.A.,
RA   Draper I., Walter G.A., Kang P.B.;
RT   "A form of muscular dystrophy associated with pathogenic variants in
RT   JAG2.";
RL   Am. J. Hum. Genet. 108:840-856(2021).
RN   [7]
RP   ERRATUM OF PUBMED:33861953.
RX   PubMed=34087166; DOI=10.1016/j.ajhg.2021.04.018;
RA   Coppens S., Barnard A.M., Puusepp S., Pajusalu S., Ounap K.,
RA   Vargas-Franco D., Bruels C.C., Donkervoort S., Pais L., Chao K.R.,
RA   Goodrich J.K., England E.M., Weisburd B., Ganesh V.S., Gudmundsson S.,
RA   O'Donnell-Luria A., Nigul M., Ilves P., Mohassel P., Siddique T.,
RA   Milone M., Nicolau S., Maroofian R., Houlden H., Hanna M.G., Quinlivan R.,
RA   Toosi M.B., Karimiani E.G., Costagliola S., Deconinck N., Kadhim H.,
RA   Macke E., Lanpher B.C., Klee E.W., Lusakowska A., Kostera-Pruszczyk A.,
RA   Hahn A., Schrank B., Nishino I., Ogasawara M., El Sherif R., Stojkovic T.,
RA   Nelson I., Bonne G., Cohen E., Boland-Auge A., Deleuze J.F., Meng Y.,
RA   Toepf A., Vilain C., Pacak C.A., Rivera-Zengotita M.L., Boennemann C.G.,
RA   Straub V., Handford P.A., Draper I., Walter G.A., Kang P.B.;
RL   Am. J. Hum. Genet. 108:1164-1164(2021).
CC   -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC       signaling. Involved in limb development (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9Y219; Q5VTD9: GFI1B; NbExp=2; IntAct=EBI-946223, EBI-946212;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q9Y219-1; Sequence=Displayed;
CC       Name=Short; Synonyms=HJAG2.del-E6;
CC         IsoId=Q9Y219-2; Sequence=VSP_001395;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, placenta and skeletal muscle
CC       and to a lesser extent in pancreas. Very low expression in brain, lung,
CC       liver and kidney.
CC   -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 27
CC       (LGMDR27) [MIM:619566]: An autosomal recessive muscular disorder
CC       characterized by progressive muscle weakness most prominent in the
CC       proximal lower limb and axial muscles, and resulting in walking
CC       difficulty or loss of ambulation. Additional more variable features
CC       include neck muscle weakness, scoliosis, and joint contractures. Some
CC       affected individuals manifest impaired intellectual development or
CC       speech delay, cardiomyopathy, and cardiac arrhythmia. Muscle biopsy
CC       shows non-specific dystrophic changes. {ECO:0000269|PubMed:33861953}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/41030/JAG2";
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DR   EMBL; AF020201; AAB71189.1; -; mRNA.
DR   EMBL; AF003521; AAB61285.1; -; mRNA.
DR   EMBL; AF029778; AAB84215.1; -; mRNA.
DR   EMBL; AF029779; AAB84216.1; -; mRNA.
DR   EMBL; AF111170; AAD15562.1; -; Genomic_DNA.
DR   EMBL; Y14330; CAA74706.1; -; mRNA.
DR   CCDS; CCDS9998.1; -. [Q9Y219-1]
DR   CCDS; CCDS9999.1; -. [Q9Y219-2]
DR   RefSeq; NP_002217.3; NM_002226.4. [Q9Y219-1]
DR   RefSeq; NP_660142.1; NM_145159.2. [Q9Y219-2]
DR   PDB; 5MW5; X-ray; 2.70 A; A=27-309.
DR   PDB; 5MW7; X-ray; 2.80 A; A=27-348.
DR   PDB; 5MWF; X-ray; 2.80 A; A/B/C/D/E/F=27-309.
DR   PDBsum; 5MW5; -.
DR   PDBsum; 5MW7; -.
DR   PDBsum; 5MWF; -.
DR   AlphaFoldDB; Q9Y219; -.
DR   SMR; Q9Y219; -.
DR   BioGRID; 109918; 152.
DR   IntAct; Q9Y219; 20.
DR   MINT; Q9Y219; -.
DR   STRING; 9606.ENSP00000328169; -.
DR   GlyCosmos; Q9Y219; 5 sites, No reported glycans.
DR   GlyGen; Q9Y219; 5 sites.
DR   iPTMnet; Q9Y219; -.
DR   PhosphoSitePlus; Q9Y219; -.
DR   SwissPalm; Q9Y219; -.
DR   BioMuta; JAG2; -.
DR   DMDM; 116242598; -.
DR   EPD; Q9Y219; -.
DR   jPOST; Q9Y219; -.
DR   MassIVE; Q9Y219; -.
DR   MaxQB; Q9Y219; -.
DR   PaxDb; 9606-ENSP00000328169; -.
DR   PeptideAtlas; Q9Y219; -.
DR   ProteomicsDB; 85595; -. [Q9Y219-1]
DR   ProteomicsDB; 85596; -. [Q9Y219-2]
DR   ABCD; Q9Y219; 20 sequenced antibodies.
DR   Antibodypedia; 14930; 503 antibodies from 38 providers.
DR   DNASU; 3714; -.
DR   Ensembl; ENST00000331782.8; ENSP00000328169.3; ENSG00000184916.9. [Q9Y219-1]
DR   Ensembl; ENST00000347004.2; ENSP00000328566.2; ENSG00000184916.9. [Q9Y219-2]
DR   GeneID; 3714; -.
DR   KEGG; hsa:3714; -.
DR   MANE-Select; ENST00000331782.8; ENSP00000328169.3; NM_002226.5; NP_002217.3.
DR   UCSC; uc001yqg.4; human. [Q9Y219-1]
DR   AGR; HGNC:6189; -.
DR   CTD; 3714; -.
DR   DisGeNET; 3714; -.
DR   GeneCards; JAG2; -.
DR   HGNC; HGNC:6189; JAG2.
DR   HPA; ENSG00000184916; Low tissue specificity.
DR   MalaCards; JAG2; -.
DR   MIM; 602570; gene.
DR   MIM; 619566; phenotype.
DR   neXtProt; NX_Q9Y219; -.
DR   OpenTargets; ENSG00000184916; -.
DR   PharmGKB; PA29987; -.
DR   VEuPathDB; HostDB:ENSG00000184916; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   GeneTree; ENSGT00940000160944; -.
DR   HOGENOM; CLU_004732_0_0_1; -.
DR   InParanoid; Q9Y219; -.
DR   OMA; KGTNCHI; -.
DR   OrthoDB; 5475408at2759; -.
DR   PhylomeDB; Q9Y219; -.
DR   TreeFam; TF351835; -.
DR   PathwayCommons; Q9Y219; -.
DR   Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2660826; Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant.
DR   Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR   SignaLink; Q9Y219; -.
DR   SIGNOR; Q9Y219; -.
DR   BioGRID-ORCS; 3714; 15 hits in 1165 CRISPR screens.
DR   ChiTaRS; JAG2; human.
DR   GeneWiki; JAG2; -.
DR   GenomeRNAi; 3714; -.
DR   Pharos; Q9Y219; Tbio.
DR   PRO; PR:Q9Y219; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9Y219; Protein.
DR   Bgee; ENSG00000184916; Expressed in nipple and 202 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IDA:UniProtKB.
DR   GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR   GO; GO:0009912; P:auditory receptor cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
DR   GO; GO:1990134; P:epithelial cell apoptotic process involved in palatal shelf morphogenesis; IEA:Ensembl.
DR   GO; GO:0042492; P:gamma-delta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; NAS:UniProtKB.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0003016; P:respiratory system process; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
DR   GO; GO:0030217; P:T cell differentiation; IDA:UniProtKB.
DR   GO; GO:0045061; P:thymic T cell selection; IDA:UniProtKB.
DR   CDD; cd00054; EGF_CA; 13.
DR   Gene3D; 2.10.25.140; -; 1.
DR   Gene3D; 2.60.40.3510; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 15.
DR   InterPro; IPR001774; DSL.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR026219; Jagged/Serrate.
DR   InterPro; IPR011651; Notch_ligand_N.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR   PANTHER; PTHR24044:SF421; PROTEIN JAGGED-2; 1.
DR   Pfam; PF21700; DL-JAG_EGF-like; 1.
DR   Pfam; PF01414; DSL; 1.
DR   Pfam; PF00008; EGF; 9.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF12661; hEGF; 3.
DR   Pfam; PF07657; MNNL; 1.
DR   PRINTS; PR00010; EGFBLOOD.
DR   PRINTS; PR02059; JAGGEDFAMILY.
DR   SMART; SM00051; DSL; 1.
DR   SMART; SM00181; EGF; 16.
DR   SMART; SM00179; EGF_CA; 14.
DR   SMART; SM00214; VWC; 1.
DR   SMART; SM00215; VWC_out; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 6.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 10.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 16.
DR   PROSITE; PS01186; EGF_2; 12.
DR   PROSITE; PS50026; EGF_3; 15.
DR   PROSITE; PS01187; EGF_CA; 8.
DR   PROSITE; PS50184; VWFC_2; 1.
DR   Genevisible; Q9Y219; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Developmental protein;
KW   Disease variant; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Limb-girdle muscular dystrophy; Membrane; Notch signaling pathway;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1238
FT                   /note="Protein jagged-2"
FT                   /id="PRO_0000007629"
FT   TOPO_DOM        27..1080
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1081..1101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1102..1238
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          196..240
FT                   /note="DSL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00377"
FT   DOMAIN          241..274
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          275..305
FT                   /note="EGF-like 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          307..345
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          347..383
FT                   /note="EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          385..421
FT                   /note="EGF-like 5; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          423..459
FT                   /note="EGF-like 6; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          461..496
FT                   /note="EGF-like 7; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          498..534
FT                   /note="EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          536..572
FT                   /note="EGF-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          574..634
FT                   /note="EGF-like 10; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          636..672
FT                   /note="EGF-like 11; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          674..710
FT                   /note="EGF-like 12; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          712..748
FT                   /note="EGF-like 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          751..787
FT                   /note="EGF-like 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          789..825
FT                   /note="EGF-like 15; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          827..863
FT                   /note="EGF-like 16; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          870..944
FT                   /note="VWFC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   REGION          1114..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1156..1238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1188..1207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        570
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        619
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        752
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1058
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        198..207
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..223
FT                   /evidence="ECO:0000250"
FT   DISULFID        231..240
FT                   /evidence="ECO:0000250"
FT   DISULFID        245..256
FT                   /evidence="ECO:0000250"
FT   DISULFID        249..262
FT                   /evidence="ECO:0000250"
FT   DISULFID        264..273
FT                   /evidence="ECO:0000250"
FT   DISULFID        276..287
FT                   /evidence="ECO:0000250"
FT   DISULFID        282..293
FT                   /evidence="ECO:0000250"
FT   DISULFID        295..304
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..323
FT                   /evidence="ECO:0000250"
FT   DISULFID        317..333
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..344
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..362
FT                   /evidence="ECO:0000250"
FT   DISULFID        356..371
FT                   /evidence="ECO:0000250"
FT   DISULFID        373..382
FT                   /evidence="ECO:0000250"
FT   DISULFID        389..400
FT                   /evidence="ECO:0000250"
FT   DISULFID        394..409
FT                   /evidence="ECO:0000250"
FT   DISULFID        411..420
FT                   /evidence="ECO:0000250"
FT   DISULFID        427..438
FT                   /evidence="ECO:0000250"
FT   DISULFID        432..447
FT                   /evidence="ECO:0000250"
FT   DISULFID        449..458
FT                   /evidence="ECO:0000250"
FT   DISULFID        465..475
FT                   /evidence="ECO:0000250"
FT   DISULFID        469..484
FT                   /evidence="ECO:0000250"
FT   DISULFID        486..495
FT                   /evidence="ECO:0000250"
FT   DISULFID        502..513
FT                   /evidence="ECO:0000250"
FT   DISULFID        507..522
FT                   /evidence="ECO:0000250"
FT   DISULFID        524..533
FT                   /evidence="ECO:0000250"
FT   DISULFID        540..551
FT                   /evidence="ECO:0000250"
FT   DISULFID        545..560
FT                   /evidence="ECO:0000250"
FT   DISULFID        562..571
FT                   /evidence="ECO:0000250"
FT   DISULFID        589..612
FT                   /evidence="ECO:0000255"
FT   DISULFID        606..622
FT                   /evidence="ECO:0000255"
FT   DISULFID        624..633
FT                   /evidence="ECO:0000250"
FT   DISULFID        640..651
FT                   /evidence="ECO:0000250"
FT   DISULFID        645..660
FT                   /evidence="ECO:0000250"
FT   DISULFID        662..671
FT                   /evidence="ECO:0000250"
FT   DISULFID        678..689
FT                   /evidence="ECO:0000250"
FT   DISULFID        683..698
FT                   /evidence="ECO:0000250"
FT   DISULFID        700..709
FT                   /evidence="ECO:0000250"
FT   DISULFID        716..727
FT                   /evidence="ECO:0000250"
FT   DISULFID        721..736
FT                   /evidence="ECO:0000250"
FT   DISULFID        738..747
FT                   /evidence="ECO:0000250"
FT   DISULFID        755..766
FT                   /evidence="ECO:0000250"
FT   DISULFID        760..775
FT                   /evidence="ECO:0000250"
FT   DISULFID        777..786
FT                   /evidence="ECO:0000250"
FT   DISULFID        793..804
FT                   /evidence="ECO:0000250"
FT   DISULFID        798..813
FT                   /evidence="ECO:0000250"
FT   DISULFID        815..824
FT                   /evidence="ECO:0000250"
FT   DISULFID        831..842
FT                   /evidence="ECO:0000250"
FT   DISULFID        836..851
FT                   /evidence="ECO:0000250"
FT   DISULFID        853..862
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         424..461
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:10662552"
FT                   /id="VSP_001395"
FT   VARIANT         74
FT                   /note="C -> S (in LGMDR27; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086389"
FT   VARIANT         95
FT                   /note="T -> A (in LGMDR27; uncertain significance;
FT                   dbSNP:rs1555371784)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086390"
FT   VARIANT         164
FT                   /note="E -> K (in LGMDR27; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086391"
FT   VARIANT         165..1238
FT                   /note="Missing (in LGMDR27)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086392"
FT   VARIANT         243
FT                   /note="A -> D (in LGMDR27; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086393"
FT   VARIANT         358
FT                   /note="N -> I (in LGMDR27; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086394"
FT   VARIANT         501
FT                   /note="E -> K (in dbSNP:rs1057744)"
FT                   /evidence="ECO:0000269|PubMed:10079256,
FT                   ECO:0000269|PubMed:10662552, ECO:0000269|PubMed:9315665"
FT                   /id="VAR_028113"
FT   VARIANT         538
FT                   /note="D -> N (in dbSNP:rs9972231)"
FT                   /id="VAR_048986"
FT   VARIANT         682
FT                   /note="P -> S (in LGMDR27; uncertain significance;
FT                   dbSNP:rs200708284)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086395"
FT   VARIANT         702
FT                   /note="Missing (in LGMDR27; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086396"
FT   VARIANT         712
FT                   /note="R -> C (in LGMDR27; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086397"
FT   VARIANT         825
FT                   /note="R -> C (in LGMDR27; uncertain significance;
FT                   dbSNP:rs1459726266)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086398"
FT   VARIANT         839
FT                   /note="G -> R (in LGMDR27; dbSNP:rs781734780)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086399"
FT   VARIANT         977
FT                   /note="F -> S (in LGMDR27; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33861953"
FT                   /id="VAR_086400"
FT   CONFLICT        8..12
FT                   /note="RLPRR -> AFPPA (in Ref. 1; AAB71189)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="A -> P (in Ref. 1; AAB71189)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="L -> F (in Ref. 1; AAB71189)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384
FT                   /note="L -> SA (in Ref. 4; CAA74706)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        424..426
FT                   /note="ANE -> VND (in Ref. 1; AAB71189)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1235
FT                   /note="A -> V (in Ref. 2; AAB61285)"
FT                   /evidence="ECO:0000305"
FT   STRAND          28..38
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          69..76
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          99..104
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:5MW7"
FT   HELIX           113..118
FT                   /evidence="ECO:0007829|PDB:5MW7"
FT   STRAND          129..134
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          140..150
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          162..171
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          179..184
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          189..198
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          214..216
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          219..223
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          268..273
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          284..286
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   TURN            301..304
FT                   /evidence="ECO:0007829|PDB:5MW5"
FT   STRAND          306..314
FT                   /evidence="ECO:0007829|PDB:5MW7"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:5MW7"
FT   STRAND          331..333
FT                   /evidence="ECO:0007829|PDB:5MW7"
SQ   SEQUENCE   1238 AA;  133367 MW;  23B4FCD7D2891EF7 CRC64;
     MRAQGRGRLP RRLLLLLALW VQAARPMGYF ELQLSALRNV NGELLSGACC DGDGRTTRAG
     GCGHDECDTY VRVCLKEYQA KVTPTGPCSY GHGATPVLGG NSFYLPPAGA AGDRARARAR
     AGGDQDPGLV VIPFQFAWPR SFTLIVEAWD WDNDTTPNEE LLIERVSHAG MINPEDRWKS
     LHFSGHVAHL ELQIRVRCDE NYYSATCNKF CRPRNDFFGH YTCDQYGNKA CMDGWMGKEC
     KEAVCKQGCN LLHGGCTVPG ECRCSYGWQG RFCDECVPYP GCVHGSCVEP WQCNCETNWG
     GLLCDKDLNY CGSHHPCTNG GTCINAEPDQ YRCTCPDGYS GRNCEKAEHA CTSNPCANGG
     SCHEVPSGFE CHCPSGWSGP TCALDIDECA SNPCAAGGTC VDQVDGFECI CPEQWVGATC
     QLDANECEGK PCLNAFSCKN LIGGYYCDCI PGWKGINCHI NVNDCRGQCQ HGGTCKDLVN
     GYQCVCPRGF GGRHCELERD ECASSPCHSG GLCEDLADGF HCHCPQGFSG PLCEVDVDLC
     EPSPCRNGAR CYNLEGDYYC ACPDDFGGKN CSVPREPCPG GACRVIDGCG SDAGPGMPGT
     AASGVCGPHG RCVSQPGGNF SCICDSGFTG TYCHENIDDC LGQPCRNGGT CIDEVDAFRC
     FCPSGWEGEL CDTNPNDCLP DPCHSRGRCY DLVNDFYCAC DDGWKGKTCH SREFQCDAYT
     CSNGGTCYDS GDTFRCACPP GWKGSTCAVA KNSSCLPNPC VNGGTCVGSG ASFSCICRDG
     WEGRTCTHNT NDCNPLPCYN GGICVDGVNW FRCECAPGFA GPDCRINIDE CQSSPCAYGA
     TCVDEINGYR CSCPPGRAGP RCQEVIGFGR SCWSRGTPFP HGSSWVEDCN SCRCLDGRRD
     CSKVWCGWKP CLLAGQPEAL SAQCPLGQRC LEKAPGQCLR PPCEAWGECG AEEPPSTPCL
     PRSGHLDNNC ARLTLHFNRD HVPQGTTVGA ICSGIRSLPA TRAVARDRLL VLLCDRASSG
     ASAVEVAVSF SPARDLPDSS LIQGAAHAIV AAITQRGNSS LLLAVTEVKV ETVVTGGSST
     GLLVPVLCGA FSVLWLACVV LCVWWTRKRR KERERSRLPR EESANNQWAP LNPIRNPIER
     PGGHKDVLYQ CKNFTPPPRR ADEALPGPAG HAAVREDEED EDLGRGEEDS LEAEKFLSHK
     FTKDPGRSPG RPAHWASGPK VDNRAVRSIN EARYAGKE
//