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   27-MAR-2024, entry version 162.
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   GlyCosmos; Q8TER0; 15 sites, 1 glycan.
DR   GlyGen; Q8TER0; 17 sites, 2 O-linked glycans (3 sites).
DR   iPTMnet; Q8TER0; -.
DR   PhosphoSitePlus; Q8TER0; -.
DR   BioMuta; SNED1; -.
DR   DMDM; 158563933; -.
DR   EPD; Q8TER0; -.
DR   jPOST; Q8TER0; -.
DR   MassIVE; Q8TER0; -.
DR   PaxDb; 9606-ENSP00000308893; -.
DR   PeptideAtlas; Q8TER0; -.
DR   ProteomicsDB; 74481; -. [Q8TER0-1]
DR   ProteomicsDB; 74482; -. [Q8TER0-3]
DR   ProteomicsDB; 74483; -. [Q8TER0-4]
DR   ProteomicsDB; 74484; -. [Q8TER0-5]
DR   Antibodypedia; 34540; 82 antibodies from 16 providers.
DR   DNASU; 25992; -.
DR   Ensembl; ENST00000310397.13; ENSP00000308893.8; ENSG00000162804.15. [Q8TER0-1]
DR   Ensembl; ENST00000401884.5; ENSP00000384871.1; ENSG00000162804.15. [Q8TER0-5]
DR   Ensembl; ENST00000405547.7; ENSP00000386007.3; ENSG00000162804.15. [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   AGR; HGNC:24696; -.
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; 5475408at2759; -.
DR   PhylomeDB; Q8TER0; -.
DR   TreeFam; TF335195; -.
DR   PathwayCommons; Q8TER0; -.
DR   SignaLink; Q8TER0; -.
DR   BioGRID-ORCS; 25992; 8 hits in 1137 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 158 other cell types or tissues.
DR   ExpressionAtlas; Q8TER0; baseline and differential.
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; cd00054; EGF_CA; 12.
DR   CDD; cd00063; FN3; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 2.10.25.10; Laminin; 15.
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   PANTHER; PTHR24044; NOTCH LIGAND FAMILY MEMBER; 1.
DR   Pfam; PF00008; EGF; 11.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF12661; hEGF; 3.
DR   Pfam; PF06119; NIDO; 1.
DR   PRINTS; PR00010; EGFBLOOD.
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; SSF57535; Complement control module/SCR domain; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 15.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
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.
DR   Genevisible; Q8TER0; HS.
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
//