CREL2_HUMAN
ID CREL2_HUMAN Reviewed; 353 AA.
AC Q6UXH1; A5GZA2; A5GZA3; A5GZA4; A5GZA5; A5GZA6; Q4W0V0; Q86UC0; Q9BU47;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein disulfide isomerase CRELD2 {ECO:0000305};
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:Q9CYA0};
DE AltName: Full=Cysteine-rich with EGF-like domain protein 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=CRELD2; ORFNames=UNQ185/PRO211;
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 3), FUNCTION, INTERACTION WITH CHRNA4,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=16238698; DOI=10.1111/j.1471-4159.2005.03473.x;
RA Ortiz J.A., Castillo M., Dominguez del Toro E., Mulet J., Gerber S.,
RA Valor L.M., Sala S., Sala F., Gutierrez L.M., Criado M.;
RT "The cysteine-rich with EGF-like domains 2 (CRELD2) protein interacts with
RT the large cytoplasmic domain of human neuronal nicotinic acetylcholine
RT receptor alpha4 and beta2 subunits.";
RL J. Neurochem. 95:1585-1596(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5 AND 6), ALTERNATIVE
RP SPLICING (ISOFORMS 1; 2; 3; 4; 5 AND 6), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16919896; DOI=10.1016/j.gene.2006.06.016;
RA Maslen C.L., Babcock D., Redig J.K., Kapeli K., Akkari Y.M., Olson S.B.;
RT "CRELD2: gene mapping, alternate splicing, and comparative genomic
RT identification of the promoter region.";
RL Gene 382:111-120(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP ALA-295 AND GLY-325.
RC TISSUE=Lung carcinoma, and Pancreatic carcinoma;
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 PROTEIN SEQUENCE OF 25-39.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Protein disulfide isomerase (By similarity). Might play a
CC role in the unfolded protein response (By similarity). May regulate
CC transport of alpha4-beta2 neuronal acetylcholine receptor
CC (PubMed:16238698). {ECO:0000250|UniProtKB:Q9CYA0,
CC ECO:0000269|PubMed:16238698}.
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 -!- SUBUNIT: Interacts with CHRNA4 (PubMed:16238698). Component of a
CC complex containing at least CRELD2, MANF, MATN3 and PDIA4 (By
CC similarity). {ECO:0000250|UniProtKB:Q9CYA0,
CC ECO:0000269|PubMed:16238698}.
CC -!- INTERACTION:
CC Q6UXH1; P42771: CDKN2A; NbExp=2; IntAct=EBI-3935314, EBI-375053;
CC Q6UXH1-1; P43681: CHRNA4; NbExp=3; IntAct=EBI-21348071, EBI-7132379;
CC Q6UXH1-2; P27797: CALR; NbExp=3; IntAct=EBI-21670927, EBI-1049597;
CC Q6UXH1-2; P12830: CDH1; NbExp=3; IntAct=EBI-21670927, EBI-727477;
CC Q6UXH1-2; Q15078: CDK5R1; NbExp=3; IntAct=EBI-21670927, EBI-746189;
CC Q6UXH1-2; P36957: DLST; NbExp=3; IntAct=EBI-21670927, EBI-351007;
CC Q6UXH1-2; P42858: HTT; NbExp=6; IntAct=EBI-21670927, EBI-466029;
CC Q6UXH1-2; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-21670927, EBI-1055945;
CC Q6UXH1-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-21670927, EBI-25882629;
CC Q6UXH1-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-21670927, EBI-5235340;
CC Q6UXH1-2; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-21670927, EBI-11952721;
CC Q6UXH1-3; P43681: CHRNA4; NbExp=3; IntAct=EBI-21348090, EBI-7132379;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:16238698}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Delta;
CC IsoId=Q6UXH1-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q6UXH1-2; Sequence=VSP_021341;
CC Name=3; Synonyms=Beta;
CC IsoId=Q6UXH1-3; Sequence=VSP_021342, VSP_021343;
CC Name=4; Synonyms=Gamma;
CC IsoId=Q6UXH1-4; Sequence=VSP_021340;
CC Name=5; Synonyms=Epsilon;
CC IsoId=Q6UXH1-5; Sequence=VSP_021339;
CC Name=6; Synonyms=Zeta;
CC IsoId=Q6UXH1-6; Sequence=VSP_021344;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:16238698). Highly
CC expressed in skeletal muscle, heart, liver, kidney and placenta
CC (PubMed:16238698). {ECO:0000269|PubMed:16238698,
CC ECO:0000269|PubMed:16919896}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all fetal tissues tested.
CC {ECO:0000269|PubMed:16919896}.
CC -!- MISCELLANEOUS: [Isoform 3]: Minor isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRELD family. {ECO:0000305}.
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DR EMBL; AJ968414; CAI91316.1; -; mRNA.
DR EMBL; DQ470676; ABF06668.1; -; mRNA.
DR EMBL; DQ470677; ABF06669.1; -; mRNA.
DR EMBL; DQ470678; ABF06670.1; -; mRNA.
DR EMBL; DQ470679; ABF06671.1; -; mRNA.
DR EMBL; DQ470680; ABF06672.1; -; mRNA.
DR EMBL; AY358355; AAQ88721.1; -; mRNA.
DR EMBL; AL671710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471138; EAW73483.1; -; Genomic_DNA.
DR EMBL; CH471138; EAW73484.1; -; Genomic_DNA.
DR EMBL; BC002894; AAH02894.1; -; mRNA.
DR EMBL; BC050675; AAH50675.1; -; mRNA.
DR CCDS; CCDS14082.1; -. [Q6UXH1-1]
DR CCDS; CCDS46730.1; -. [Q6UXH1-5]
DR CCDS; CCDS63515.1; -. [Q6UXH1-2]
DR CCDS; CCDS63516.1; -. [Q6UXH1-4]
DR RefSeq; NP_001128573.1; NM_001135101.2. [Q6UXH1-5]
DR RefSeq; NP_001271246.1; NM_001284317.1. [Q6UXH1-4]
DR RefSeq; NP_001271247.1; NM_001284318.1. [Q6UXH1-2]
DR RefSeq; NP_077300.3; NM_024324.4. [Q6UXH1-1]
DR RefSeq; XP_005261795.1; XM_005261738.4. [Q6UXH1-6]
DR AlphaFoldDB; Q6UXH1; -.
DR BioGRID; 122591; 107.
DR IntAct; Q6UXH1; 48.
DR MINT; Q6UXH1; -.
DR GlyConnect; 1164; 7 N-Linked glycans (2 sites).
DR GlyGen; Q6UXH1; 3 sites, 7 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q6UXH1; -.
DR PhosphoSitePlus; Q6UXH1; -.
DR BioMuta; CRELD2; -.
DR DMDM; 74738218; -.
DR EPD; Q6UXH1; -.
DR jPOST; Q6UXH1; -.
DR MassIVE; Q6UXH1; -.
DR MaxQB; Q6UXH1; -.
DR PeptideAtlas; Q6UXH1; -.
DR PRIDE; Q6UXH1; -.
DR ProteomicsDB; 67616; -. [Q6UXH1-1]
DR ProteomicsDB; 67617; -. [Q6UXH1-2]
DR ProteomicsDB; 67618; -. [Q6UXH1-3]
DR ProteomicsDB; 67619; -. [Q6UXH1-4]
DR ProteomicsDB; 67620; -. [Q6UXH1-5]
DR ProteomicsDB; 67621; -. [Q6UXH1-6]
DR Antibodypedia; 200; 211 antibodies from 25 providers.
DR DNASU; 79174; -.
DR Ensembl; ENST00000328268.9; ENSP00000332223.4; ENSG00000184164.15. [Q6UXH1-1]
DR Ensembl; ENST00000403427.3; ENSP00000384111.3; ENSG00000184164.15. [Q6UXH1-4]
DR Ensembl; ENST00000404488.7; ENSP00000383938.3; ENSG00000184164.15. [Q6UXH1-5]
DR Ensembl; ENST00000407217.7; ENSP00000386034.3; ENSG00000184164.15. [Q6UXH1-2]
DR GeneID; 79174; -.
DR KEGG; hsa:79174; -.
DR MANE-Select; ENST00000328268.9; ENSP00000332223.4; NM_024324.5; NP_077300.3.
DR UCSC; uc003bja.4; human. [Q6UXH1-1]
DR CTD; 79174; -.
DR DisGeNET; 79174; -.
DR GeneCards; CRELD2; -.
DR HGNC; HGNC:28150; CRELD2.
DR HPA; ENSG00000184164; Low tissue specificity.
DR MIM; 607171; gene.
DR neXtProt; NX_Q6UXH1; -.
DR OpenTargets; ENSG00000184164; -.
DR PharmGKB; PA142672079; -.
DR VEuPathDB; HostDB:ENSG00000184164; -.
DR GeneTree; ENSGT00940000160071; -.
DR HOGENOM; CLU_038974_1_0_1; -.
DR InParanoid; Q6UXH1; -.
DR OMA; DQEACVD; -.
DR OrthoDB; 883628at2759; -.
DR PhylomeDB; Q6UXH1; -.
DR TreeFam; TF316507; -.
DR PathwayCommons; Q6UXH1; -.
DR SignaLink; Q6UXH1; -.
DR BioGRID-ORCS; 79174; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; CRELD2; human.
DR GeneWiki; CRELD2; -.
DR GenomeRNAi; 79174; -.
DR Pharos; Q6UXH1; Tbio.
DR PRO; PR:Q6UXH1; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q6UXH1; protein.
DR Bgee; ENSG00000184164; Expressed in secondary oocyte and 200 other tissues.
DR ExpressionAtlas; Q6UXH1; baseline and differential.
DR Genevisible; Q6UXH1; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR CDD; cd00064; FU; 2.
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; 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; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 25..353
FT /note="Protein disulfide isomerase CRELD2"
FT /id="PRO_0000256244"
FT DOMAIN 136..178
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 193..240
FT /note="FU 1"
FT REPEAT 253..302
FT /note="FU 2"
FT DOMAIN 290..331
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 332..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 31..34
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT MOTIF 263..266
FT /note="CXXC"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..34
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT DISULFID 140..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 148..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 168..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 263..266
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q9CYA0"
FT DISULFID 294..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 301..317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 319..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 197
FT /note="T -> TVRTGLSDSYPPCCLSLGCWRGVGHAWIRGRNTHTQPGYSSRVWIAA
FT FSP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16919896"
FT /id="VSP_021339"
FT VAR_SEQ 230..257
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16919896"
FT /id="VSP_021340"
FT VAR_SEQ 258..289
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16919896"
FT /id="VSP_021341"
FT VAR_SEQ 258..284
FT /note="ECDSSCVGCTGEGPGNCKECISGYARE -> GGPGGRVCTPGPAGFRCCLCQ
FT HSFMAS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16238698"
FT /id="VSP_021342"
FT VAR_SEQ 285..353
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16238698"
FT /id="VSP_021343"
FT VAR_SEQ 337..353
FT /note="EATEGESPTQLPSREDL -> GEWHGCPPHRLPSPGPQGLHVDWLLGLKSTQ
FT MVALRW (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16919896"
FT /id="VSP_021344"
FT VARIANT 182
FT /note="D -> E (in dbSNP:rs8139422)"
FT /id="VAR_028892"
FT VARIANT 295
FT /note="S -> A (in dbSNP:rs11545762)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028893"
FT VARIANT 325
FT /note="E -> G (in dbSNP:rs11545763)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028894"
SQ SEQUENCE 353 AA; 38192 MW; ED8C635DD74E768D CRC64;
MRLPRRAALG LLPLLLLLPP APEAAKKPTP CHRCRGLVDK FNQGMVDTAK KNFGGGNTAW
EEKTLSKYES SEIRLLEILE GLCESSDFEC NQMLEAQEEH LEAWWLQLKS EYPDLFEWFC
VKTLKVCCSP GTYGPDCLAC QGGSQRPCSG NGHCSGDGSR QGDGSCRCHM GYQGPLCTDC
MDGYFSSLRN ETHSICTACD ESCKTCSGLT NRDCGECEVG WVLDEGACVD VDECAAEPPP
CSAAQFCKNA NGSYTCEECD SSCVGCTGEG PGNCKECISG YAREHGQCAD VDECSLAEKT
CVRKNENCYN TPGSYVCVCP DGFEETEDAC VPPAEAEATE GESPTQLPSR EDL
