CREL1_HUMAN
ID CREL1_HUMAN Reviewed; 420 AA.
AC Q96HD1; A8MX90; B2RAA9; Q6I9X5; Q8NFT4; Q9Y409;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein disulfide isomerase CRELD1 {ECO:0000305};
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:Q9CYA0};
DE AltName: Full=Cysteine-rich with EGF-like domain protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=CRELD1; Synonyms=CIRRIN; ORFNames=UNQ188/PRO214;
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), TISSUE SPECIFICITY, AND VARIANT
RP VAL-13.
RC TISSUE=Fibroblast;
RX PubMed=12137942; DOI=10.1016/s0378-1119(02)00696-0;
RA Rupp P.A., Fouad G.T., Egelston C.A., Reifsteck C.A., Olson S.B.,
RA Knosp W.M., Glanville R.W., Thornburg K.L., Robinson S.W., Maslen C.L.;
RT "Identification, genomic organization and mRNA expression of CRELD1, the
RT founding member of a unique family of matricellular proteins.";
RL Gene 293:47-57(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-13.
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-13.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-13.
RC TISSUE=Amygdala;
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] (ISOFORM 2), AND VARIANT VAL-13.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-13.
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 [8]
RP INDUCTION.
RX PubMed=23027870; DOI=10.1074/jbc.m112.405050;
RA Hansen H.G., Schmidt J.D., Soltoft C.L., Ramming T., Geertz-Hansen H.M.,
RA Christensen B., Sorensen E.S., Juncker A.S., Appenzeller-Herzog C.,
RA Ellgaard L.;
RT "Hyperactivity of the Ero1alpha oxidase elicits endoplasmic reticulum
RT stress but no broad antioxidant response.";
RL J. Biol. Chem. 287:39513-39523(2012).
RN [9]
RP VARIANTS AVSD2 HIS-107; ILE-311 AND CYS-329.
RX PubMed=12632326; DOI=10.1086/374319;
RA Robinson S.W., Morris C.D., Goldmuntz E., Reller M.D., Jones M.A.,
RA Steiner R.D., Maslen C.L.;
RT "Missense mutations in CRELD1 are associated with cardiac atrioventricular
RT septal defects.";
RL Am. J. Hum. Genet. 72:1047-1052(2003).
RN [10]
RP VARIANT AVSD2 ALA-162.
RX PubMed=15857420; DOI=10.1111/j.1399-0004.2005.00435.x;
RA Zatyka M., Priestley M., Ladusans E.J., Fryer A.E., Mason J., Latif F.,
RA Maher E.R.;
RT "Analysis of CRELD1 as a candidate 3p25 atrioventicular septal defect locus
RT (AVSD2).";
RL Clin. Genet. 67:526-528(2005).
CC -!- FUNCTION: Protein disulfide isomerase (By similarity). Promotes the
CC localization of acetylcholine receptors (AChRs) to the plasma membrane
CC (By similarity). {ECO:0000250|UniProtKB:Q91XD7,
CC ECO:0000250|UniProtKB:Q9CYA0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:Q9CYA0};
CC -!- INTERACTION:
CC Q96HD1; P35348-1: ADRA1A; NbExp=3; IntAct=EBI-713009, EBI-21288891;
CC Q96HD1-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-21536433, EBI-1055254;
CC Q96HD1-2; P19404: NDUFV2; NbExp=3; IntAct=EBI-21536433, EBI-713665;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q96HD1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HD1-2; Sequence=VSP_016091;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetal lung, liver, kidney,
CC adult heart, brain and skeletal muscle. Weakly expressed in placenta,
CC fetal brain, and adult lung, liver, kidney and pancreas.
CC {ECO:0000269|PubMed:12137942}.
CC -!- INDUCTION: Up-regulated by inducers of the unfolded protein response
CC (UPR), including tunicamycin and thapsigargin.
CC {ECO:0000269|PubMed:23027870}.
CC -!- DISEASE: Atrioventricular septal defect 2 (AVSD2) [MIM:606217]: A
CC congenital heart malformation characterized by a common
CC atrioventricular junction coexisting with deficient atrioventricular
CC septation. The complete form involves underdevelopment of the lower
CC part of the atrial septum and the upper part of the ventricular septum;
CC the valve itself is also shared. A less severe form, known as ostium
CC primum atrial septal defect, is characterized by separate
CC atrioventricular valvar orifices despite a common junction.
CC {ECO:0000269|PubMed:12632326, ECO:0000269|PubMed:15857420}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CRELD family. {ECO:0000305}.
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DR EMBL; AF452623; AAM75206.1; -; mRNA.
DR EMBL; AL050275; CAB43376.1; -; mRNA.
DR EMBL; AY358363; AAQ88729.1; -; mRNA.
DR EMBL; AK314113; BAG36806.1; -; mRNA.
DR EMBL; CR457380; CAG33661.1; -; mRNA.
DR EMBL; AC018809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008720; AAH08720.1; -; mRNA.
DR CCDS; CCDS2593.1; -. [Q96HD1-1]
DR CCDS; CCDS33693.1; -. [Q96HD1-2]
DR PIR; T08724; T08724.
DR RefSeq; NP_001026887.1; NM_001031717.3. [Q96HD1-2]
DR RefSeq; NP_001070883.1; NM_001077415.2. [Q96HD1-1]
DR RefSeq; NP_056328.2; NM_015513.4. [Q96HD1-1]
DR RefSeq; XP_016862664.1; XM_017007175.1.
DR AlphaFoldDB; Q96HD1; -.
DR BioGRID; 122458; 184.
DR IntAct; Q96HD1; 28.
DR MINT; Q96HD1; -.
DR STRING; 9606.ENSP00000321856; -.
DR GlyGen; Q96HD1; 2 sites.
DR iPTMnet; Q96HD1; -.
DR PhosphoSitePlus; Q96HD1; -.
DR BioMuta; CRELD1; -.
DR DMDM; 209572751; -.
DR EPD; Q96HD1; -.
DR jPOST; Q96HD1; -.
DR MassIVE; Q96HD1; -.
DR MaxQB; Q96HD1; -.
DR PeptideAtlas; Q96HD1; -.
DR PRIDE; Q96HD1; -.
DR ProteomicsDB; 76734; -. [Q96HD1-1]
DR ProteomicsDB; 76735; -. [Q96HD1-2]
DR Antibodypedia; 25846; 127 antibodies from 24 providers.
DR DNASU; 78987; -.
DR Ensembl; ENST00000326434.9; ENSP00000321856.5; ENSG00000163703.20. [Q96HD1-2]
DR Ensembl; ENST00000383811.8; ENSP00000373322.3; ENSG00000163703.20. [Q96HD1-1]
DR Ensembl; ENST00000452070.6; ENSP00000393643.2; ENSG00000163703.20. [Q96HD1-1]
DR Ensembl; ENST00000682783.1; ENSP00000508358.1; ENSG00000163703.20. [Q96HD1-1]
DR Ensembl; ENST00000684493.1; ENSP00000507127.1; ENSG00000163703.20. [Q96HD1-1]
DR GeneID; 78987; -.
DR KEGG; hsa:78987; -.
DR MANE-Select; ENST00000452070.6; ENSP00000393643.2; NM_001077415.3; NP_001070883.2.
DR UCSC; uc003buf.4; human. [Q96HD1-1]
DR CTD; 78987; -.
DR DisGeNET; 78987; -.
DR GeneCards; CRELD1; -.
DR HGNC; HGNC:14630; CRELD1.
DR HPA; ENSG00000163703; Low tissue specificity.
DR MalaCards; CRELD1; -.
DR MIM; 606217; phenotype.
DR MIM; 607170; gene.
DR neXtProt; NX_Q96HD1; -.
DR OpenTargets; ENSG00000163703; -.
DR Orphanet; 99067; Complete atrioventricular septal defect with ventricular hypoplasia.
DR Orphanet; 99068; Complete atrioventricular septal defect-tetralogy of Fallot.
DR Orphanet; 576235; Partial atrioventricular septal defect without ventricular hypoplasia.
DR PharmGKB; PA26870; -.
DR VEuPathDB; HostDB:ENSG00000163703; -.
DR GeneTree; ENSGT00940000160255; -.
DR HOGENOM; CLU_038974_1_1_1; -.
DR InParanoid; Q96HD1; -.
DR OMA; EWLCIEQ; -.
DR OrthoDB; 883628at2759; -.
DR PhylomeDB; Q96HD1; -.
DR TreeFam; TF316507; -.
DR PathwayCommons; Q96HD1; -.
DR SignaLink; Q96HD1; -.
DR BioGRID-ORCS; 78987; 25 hits in 1079 CRISPR screens.
DR ChiTaRS; CRELD1; human.
DR GeneWiki; CRELD1; -.
DR GenomeRNAi; 78987; -.
DR Pharos; Q96HD1; Tbio.
DR PRO; PR:Q96HD1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96HD1; protein.
DR Bgee; ENSG00000163703; Expressed in right hemisphere of cerebellum and 96 other tissues.
DR ExpressionAtlas; Q96HD1; baseline and differential.
DR Genevisible; Q96HD1; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0003279; P:cardiac septum development; TAS:BHF-UCL.
DR GO; GO:0003197; P:endocardial cushion development; TAS:BHF-UCL.
DR CDD; cd00064; FU; 1.
DR InterPro; IPR021852; DUF3456.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF11938; DUF3456; 2.
DR Pfam; PF07645; EGF_CA; 2.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00261; FU; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disease variant; Disulfide bond;
KW EGF-like domain; Glycoprotein; Isomerase; Membrane; Redox-active center;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..420
FT /note="Protein disulfide isomerase CRELD1"
FT /id="PRO_0000042781"
FT TOPO_DOM 30..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..420
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 153..193
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 208..256
FT /note="FU 1"
FT REPEAT 268..315
FT /note="FU 2"
FT DOMAIN 305..344
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MOTIF 46..49
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:Q19267"
FT MOTIF 278..281
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..49
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT DISULFID 155..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 163..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 183..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 278..281
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT DISULFID 309..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 314..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 332..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 350..420
FT /note="ESAGFFSEMTEDELVVLQQMFFGIIICALATLAAKGDLVFTAIFIGAVAAMT
FT GYWLSERSDRVLEGFIKGR -> GAFPILTDLTPETTRRWKLGSHPHSTYVKMKMQRDE
FT ATFPGLYGKQVAKLGSQSRQSDRGTRLIHSQQASSQR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_016091"
FT VARIANT 13
FT /note="M -> V (in dbSNP:rs279552)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:12137942, ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5"
FT /id="VAR_046653"
FT VARIANT 107
FT /note="R -> H (in AVSD2; associated with disease
FT susceptibility; dbSNP:rs28941780)"
FT /evidence="ECO:0000269|PubMed:12632326"
FT /id="VAR_023764"
FT VARIANT 128
FT /note="P -> R (in dbSNP:rs2302787)"
FT /id="VAR_046654"
FT VARIANT 162
FT /note="P -> A (in AVSD2; associated with disease
FT susceptibility; dbSNP:rs121912626)"
FT /evidence="ECO:0000269|PubMed:15857420"
FT /id="VAR_023765"
FT VARIANT 311
FT /note="T -> I (in AVSD2; associated with disease
FT susceptibility; dbSNP:rs28942092)"
FT /evidence="ECO:0000269|PubMed:12632326"
FT /id="VAR_023766"
FT VARIANT 329
FT /note="R -> C (in AVSD2; associated with disease
FT susceptibility; dbSNP:rs28942091)"
FT /evidence="ECO:0000269|PubMed:12632326"
FT /id="VAR_023767"
FT CONFLICT 126
FT /note="E -> G (in Ref. 2; CAB43376)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="L -> P (in Ref. 5; CAG33661)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="G -> S (in Ref. 4; BAG36806)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="C -> R (in Ref. 5; CAG33661)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="Y -> C (in Ref. 2; CAB43376)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="I -> V (in Ref. 4; BAG36806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 45440 MW; EEAAD0D143A0D35A CRC64;
MAPWPPKGLV PAMLWGLSLF LNLPGPIWLQ PSPPPQSSPP PQPHPCHTCR GLVDSFNKGL
ERTIRDNFGG GNTAWEEENL SKYKDSETRL VEVLEGVCSK SDFECHRLLE LSEELVESWW
FHKQQEAPDL FQWLCSDSLK LCCPAGTFGP SCLPCPGGTE RPCGGYGQCE GEGTRGGSGH
CDCQAGYGGE ACGQCGLGYF EAERNASHLV CSACFGPCAR CSGPEESNCL QCKKGWALHH
LKCVDIDECG TEGANCGADQ FCVNTEGSYE CRDCAKACLG CMGAGPGRCK KCSPGYQQVG
SKCLDVDECE TEVCPGENKQ CENTEGGYRC ICAEGYKQME GICVKEQIPE SAGFFSEMTE
DELVVLQQMF FGIIICALAT LAAKGDLVFT AIFIGAVAAM TGYWLSERSD RVLEGFIKGR
