JAG2_HUMAN
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 03-AUG-2022, entry version 208.
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="http://atlasgeneticsoncology.org/Genes/JAG2ID41030ch14q32.html";
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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; 148.
DR IntAct; Q9Y219; 20.
DR MINT; Q9Y219; -.
DR STRING; 9606.ENSP00000328169; -.
DR GlyGen; Q9Y219; 5 sites.
DR iPTMnet; Q9Y219; -.
DR PhosphoSitePlus; Q9Y219; -.
DR BioMuta; JAG2; -.
DR DMDM; 116242598; -.
DR EPD; Q9Y219; -.
DR jPOST; Q9Y219; -.
DR MassIVE; Q9Y219; -.
DR MaxQB; Q9Y219; -.
DR PaxDb; Q9Y219; -.
DR PeptideAtlas; Q9Y219; -.
DR PRIDE; Q9Y219; -.
DR ProteomicsDB; 85595; -. [Q9Y219-1]
DR ProteomicsDB; 85596; -. [Q9Y219-2]
DR ABCD; Q9Y219; 20 sequenced antibodies.
DR Antibodypedia; 14930; 455 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 CTD; 3714; -.
DR DisGeNET; 3714; -.
DR GeneCards; JAG2; -.
DR HGNC; HGNC:6189; JAG2.
DR HPA; ENSG00000184916; Low tissue specificity.
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; YGWQGKF; -.
DR OrthoDB; 72177at2759; -.
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 1087 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 200 other tissues.
DR Genevisible; Q9Y219; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 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 Pfam; PF01414; DSL; 1.
DR Pfam; PF00008; EGF; 10.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF07657; MNNL; 1.
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; SSF57184; SSF57184; 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.
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; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33861953"
FT /id="VAR_086389"
FT VARIANT 95
FT /note="T -> A (in LGMDR27; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33861953"
FT /id="VAR_086390"
FT VARIANT 164
FT /note="E -> K (in LGMDR27; unknown pathological
FT 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; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33861953"
FT /id="VAR_086393"
FT VARIANT 358
FT /note="N -> I (in LGMDR27; unknown pathological
FT 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; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33861953"
FT /id="VAR_086395"
FT VARIANT 702
FT /note="Missing (in LGMDR27; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33861953"
FT /id="VAR_086396"
FT VARIANT 712
FT /note="R -> C (in LGMDR27; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33861953"
FT /id="VAR_086397"
FT VARIANT 825
FT /note="R -> C (in LGMDR27; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33861953"
FT /id="VAR_086398"
FT VARIANT 839
FT /note="G -> R (in LGMDR27)"
FT /evidence="ECO:0000269|PubMed:33861953"
FT /id="VAR_086399"
FT VARIANT 977
FT /note="F -> S (in LGMDR27; unknown pathological
FT 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
