SNED1_HUMAN
ID SNED1_HUMAN Reviewed; 1413 AA.
AC Q8TER0; B5MDC3; B7WNK6; B7WPM0; Q336F4; Q336F5; Q8N369; Q8TEP7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Sushi, nidogen and EGF-like domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Insulin-responsive sequence DNA-binding protein 1 {ECO:0000303|PubMed:15194686};
DE Short=IRE-BP1 {ECO:0000303|PubMed:15194686};
DE Flags: Precursor;
GN Name=SNED1 {ECO:0000303|PubMed:33724335, ECO:0000312|HGNC:HGNC:24696};
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-1413 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-1413 (ISOFORM 2).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 367-1413 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 938-1413 (ISOFORM 4).
RX PubMed=15194686; DOI=10.1074/jbc.m404349200;
RA Villafuerte B.C., Phillips L.S., Rane M.J., Zhao W.;
RT "Insulin-response element-binding protein 1: a novel Akt substrate involved
RT in transcriptional action of insulin.";
RL J. Biol. Chem. 279:36650-36659(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 791-1413 (ISOFORM 3), AND VARIANT
RP SER-1362.
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 [5]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND PHOSPHORYLATION.
RX PubMed=33724335; DOI=10.1042/bcj20200675;
RA Vallet S.D., Davis M.N., Barque A., Thahab A.H., Ricard-Blum S., Naba A.;
RT "Computational and experimental characterization of the novel ECM
RT glycoprotein SNED1 and prediction of its interactome.";
RL Biochem. J. 478:1413-1434(2021).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:33724335}. Note=Forms microfibrils within
CC the extracellular matrix and colocalizes with fibronectin (FN1).
CC {ECO:0000250|UniProtKB:Q70E20}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TER0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TER0-3; Sequence=VSP_027749, VSP_027752;
CC Name=3;
CC IsoId=Q8TER0-4; Sequence=VSP_027749, VSP_027753, VSP_027754;
CC Name=4;
CC IsoId=Q8TER0-5; Sequence=VSP_027750, VSP_027751;
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000269|PubMed:33724335}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:33724335}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27939.1; Type=Miscellaneous discrepancy; Note=Intron retention. The N-terminal region arises from intron retention.; Evidence={ECO:0000305};
CC Sequence=AAQ04558.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC005237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK074062; BAB84888.1; -; mRNA.
DR EMBL; AK074075; BAB84901.1; -; mRNA.
DR EMBL; AF439717; AAQ04558.1; ALT_INIT; mRNA.
DR EMBL; AF439718; AAQ04563.1; -; mRNA.
DR EMBL; BC027939; AAH27939.1; ALT_SEQ; mRNA.
DR CCDS; CCDS46562.1; -. [Q8TER0-1]
DR RefSeq; NP_001073906.1; NM_001080437.1. [Q8TER0-1]
DR AlphaFoldDB; Q8TER0; -.
DR SMR; Q8TER0; -.
DR BioGRID; 117471; 4.
DR IntAct; Q8TER0; 1.
DR STRING; 9606.ENSP00000308893; -.
DR GlyGen; Q8TER0; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TER0; -.
DR PhosphoSitePlus; Q8TER0; -.
DR BioMuta; SNED1; -.
DR DMDM; 158563933; -.
DR EPD; Q8TER0; -.
DR jPOST; Q8TER0; -.
DR MassIVE; Q8TER0; -.
DR PaxDb; Q8TER0; -.
DR PeptideAtlas; Q8TER0; -.
DR PRIDE; Q8TER0; -.
DR ProteomicsDB; 74481; -. [Q8TER0-1]
DR ProteomicsDB; 74482; -. [Q8TER0-3]
DR ProteomicsDB; 74483; -. [Q8TER0-4]
DR ProteomicsDB; 74484; -. [Q8TER0-5]
DR Antibodypedia; 34540; 80 antibodies from 16 providers.
DR DNASU; 25992; -.
DR Ensembl; ENST00000310397.13; ENSP00000308893.8; ENSG00000162804.14. [Q8TER0-1]
DR Ensembl; ENST00000401884.5; ENSP00000384871.1; ENSG00000162804.14. [Q8TER0-5]
DR Ensembl; ENST00000405547.7; ENSP00000386007.3; ENSG00000162804.14. [Q8TER0-3]
DR GeneID; 25992; -.
DR KEGG; hsa:25992; -.
DR MANE-Select; ENST00000310397.13; ENSP00000308893.8; NM_001080437.3; NP_001073906.1.
DR UCSC; uc002wah.2; human. [Q8TER0-1]
DR CTD; 25992; -.
DR DisGeNET; 25992; -.
DR GeneCards; SNED1; -.
DR HGNC; HGNC:24696; SNED1.
DR HPA; ENSG00000162804; Low tissue specificity.
DR MIM; 616634; gene.
DR neXtProt; NX_Q8TER0; -.
DR OpenTargets; ENSG00000162804; -.
DR PharmGKB; PA134946370; -.
DR VEuPathDB; HostDB:ENSG00000162804; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4291; Eukaryota.
DR GeneTree; ENSGT00940000160730; -.
DR HOGENOM; CLU_005107_0_0_1; -.
DR InParanoid; Q8TER0; -.
DR OMA; KAIRHRT; -.
DR OrthoDB; 7525at2759; -.
DR PhylomeDB; Q8TER0; -.
DR TreeFam; TF335195; -.
DR PathwayCommons; Q8TER0; -.
DR SignaLink; Q8TER0; -.
DR BioGRID-ORCS; 25992; 8 hits in 1059 CRISPR screens.
DR ChiTaRS; SNED1; human.
DR GenomeRNAi; 25992; -.
DR Pharos; Q8TER0; Tbio.
DR PRO; PR:Q8TER0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8TER0; protein.
DR Bgee; ENSG00000162804; Expressed in sural nerve and 156 other tissues.
DR ExpressionAtlas; Q8TER0; baseline and differential.
DR Genevisible; Q8TER0; HS.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005112; F:Notch binding; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 3.
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; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00008; EGF; 11.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF06119; NIDO; 1.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 14.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00539; NIDO; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS00022; EGF_1; 15.
DR PROSITE; PS01186; EGF_2; 13.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1413
FT /note="Sushi, nidogen and EGF-like domain-containing
FT protein 1"
FT /id="PRO_0000299554"
FT DOMAIN 103..258
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 268..309
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 311..347
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 349..385
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 352..374
FT /note="Follistatin-like 1"
FT DOMAIN 387..423
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 429..465
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 468..500
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 507..530
FT /note="Follistatin-like 2"
FT DOMAIN 541..577
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 580..616
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 619..655
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 657..693
FT /note="EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 696..753
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 753..789
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 791..827
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 829..865
FT /note="EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 867..903
FT /note="EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 908..1006
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1007..1105
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1106..1200
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1307..1343
FT /note="EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1206..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 278..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 299..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 315..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 320..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 337..346
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 353..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 358..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 375..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 391..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 396..411
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 413..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 433..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 438..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 455..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 472..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 474..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 490..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 545..556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 550..565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 567..576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 584..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 589..604
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 606..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 623..634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 628..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 645..654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 661..672
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 666..681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 683..692
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 698..739
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 724..751
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 757..768
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 762..777
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 779..788
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 795..806
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 800..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 817..826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 833..844
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 838..853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 855..864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 871..882
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 876..891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 893..902
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1311..1322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1316..1331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1333..1342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1273..1306
FT /note="QPTASAQLENMEEAPKRVSLALQLPEHGSKDIGN -> H (in isoform
FT 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_027749"
FT VAR_SEQ 1306..1324
FT /note="NVPGNCSENPCQNGGTCVP -> SESAALVGTLGLTDCSQGP (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15194686"
FT /id="VSP_027750"
FT VAR_SEQ 1325..1413
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15194686"
FT /id="VSP_027751"
FT VAR_SEQ 1375..1402
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_027752"
FT VAR_SEQ 1398
FT /note="K -> L (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027753"
FT VAR_SEQ 1399..1413
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027754"
FT VARIANT 1228
FT /note="L -> P (in dbSNP:rs17440466)"
FT /id="VAR_034847"
FT VARIANT 1289
FT /note="R -> Q (in dbSNP:rs6721345)"
FT /id="VAR_034848"
FT VARIANT 1299
FT /note="H -> R (in dbSNP:rs6708120)"
FT /id="VAR_034849"
FT VARIANT 1362
FT /note="A -> S (in dbSNP:rs2108485)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034850"
FT CONFLICT 546
FT /note="D -> N (in Ref. 3; AAQ04558)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="H -> Y (in Ref. 3; AAQ04558)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="V -> A (in Ref. 3; AAQ04558)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="S -> G (in Ref. 3; AAQ04558)"
FT /evidence="ECO:0000305"
FT CONFLICT 1186..1206
FT /note="HSEPAHLYIITSPRDGADRRW -> Q (in Ref. 3; AAQ04558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1413 AA; 152204 MW; 09BC8059234326D9 CRC64;
MRHGVAWALL VAAALGLGAR GVRGAVALAD FYPFGAERGD AVTPKQDDGG SGLRPLSVPF
PFFGAEHSGL YVNNNGIISF LKEVSQFTPV AFPIAKDRCV VAAFWADVDN RRAGDVYYRE
ATDPAMLRRA TEDVRHYFPE LLDFNATWVF VATWYRVTFF GGSSSSPVNT FQTVLITDGK
LSFTIFNYES IVWTTGTHAS SGGNATGLGG IAAQAGFNAG DGQRYFSIPG SRTADMAEVE
TTTNVGVPGR WAFRIDDAQV RVGGCGHTTS VCLALRPCLN GGKCIDDCVT GNPSYTCSCL
SGFTGRRCHL DVNECASQPC QNGGTCTHGI NSFRCQCPAG FGGPTCETAQ SPCDTKECQH
GGQCQVENGS AVCVCQAGYT GAACEMDVDD CSPDPCLNGG SCVDLVGNYT CLCAEPFKGL
RCETGDHPVP DACLSAPCHN GGTCVDADQG YVCECPEGFM GLDCRERVPD DCECRNGGRC
LGANTTLCQC PLGFFGLLCE FEITAMPCNM NTQCPDGGYC MEHGGSYLCV CHTDHNASHS
LPSPCDSDPC FNGGSCDAHD DSYTCECPRG FHGKHCEKAR PHLCSSGPCR NGGTCKEAGG
EYHCSCPYRF TGRHCEIGKP DSCASGPCHN GGTCFHYIGK YKCDCPPGFS GRHCEIAPSP
CFRSPCVNGG TCEDRDTDFF CHCQAGYMGR RCQAEVDCGP PEEVKHATLR FNGTRLGAVA
LYACDRGYSL SAPSRIRVCQ PHGVWSEPPQ CLEIDECRSQ PCLHGGSCQD RVAGYLCLCS
TGYEGAHCEL ERDECRAHPC RNGGSCRNLP GAYVCRCPAG FVGVHCETEV DACDSSPCQH
GGRCESGGGA YLCVCPESFF GYHCETVSDP CFSSPCGGRG YCLASNGSHS CTCKVGYTGE
DCAKELFPPT ALKMERVEES GVSISWNPPN GPAARQMLDG YAVTYVSSDG SYRRTDFVDR
TRSSHQLQAL AAGRAYNISV FSVKRNSNNK NDISRPAVLL ARTRPRPVEG FEVTNVTAST
ISVQWALHRI RHATVSGVRV SIRHPEALRD QATDVDRSVD RFTFRALLPG KRYTIQLTTL
SGLRGEEHPT ESLATAPTHV WTRPLPPANL TAARVTATSA HVVWDAPTPG SLLEAYVINV
TTSQSTKSRY VPNGKLASYT VRDLLPGRRY QLSVIAVQST ELGPQHSEPA HLYIITSPRD
GADRRWHQGG HHPRVLKNRP PPARLPELRL LNDHSAPETP TQPPRFSELV DGRGRVSARF
GGSPSKAATV RSQPTASAQL ENMEEAPKRV SLALQLPEHG SKDIGNVPGN CSENPCQNGG
TCVPGADAHS CDCGPGFKGR RCELACIKVS RPCTRLFSET KAFPVWEGGV CHHVYKRVYR
VHQDICFKES CESTSLKKTP NRKQSKSQTL EKS
