SCUB2_HUMAN
ID SCUB2_HUMAN Reviewed; 999 AA.
AC Q9NQ36; Q2NKQ8; Q6ZWI1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Signal peptide, CUB and EGF-like domain-containing protein 2 {ECO:0000303|PubMed:19480626};
DE AltName: Full=Protein CEGP1 {ECO:0000250|UniProtKB:Q9JJS0};
DE AltName: Full=Scube/You {ECO:0000250|UniProtKB:Q9JJS0};
DE Flags: Precursor;
GN Name=SCUBE2 {ECO:0000312|HGNC:HGNC:30425}; Synonyms=CEGP1;
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 [GENOMIC DNA] (ISOFORM 1).
RX PubMed=11528127; DOI=10.1159/000056999;
RA Amid C., Bahr A., Mujica A., Sampson N., Bikar S.E., Winterpacht A.,
RA Zabel B., Hankeln T., Schmidt E.R.;
RT "Comparative genomic sequencing reveals a strikingly similar architecture
RT of a conserved syntenic region on human chromosome 11p15.3 (including gene
RT ST5) and mouse chromosome 7.";
RL Cytogenet. Cell Genet. 93:284-290(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-591.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 TISSUE SPECIFICITY.
RX PubMed=12270931; DOI=10.1074/jbc.m207410200;
RA Yang R.-B., Ng C.K.D., Wasserman S.M., Colman S.D., Shenoy S., Mehraban F.,
RA Koemueves L.G., Tomlinson J.E., Topper J.N.;
RT "Identification of a novel family of cell-surface proteins expressed in
RT human vascular endothelium.";
RL J. Biol. Chem. 277:46364-46373(2002).
RN [6]
RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH SHH AND PTCH1, FUNCTION,
RP AND PTM.
RX PubMed=19480626; DOI=10.1042/bj20090341;
RA Tsai M.T., Cheng C.J., Lin Y.C., Chen C.C., Wu A.R., Wu M.T., Hsu C.C.,
RA Yang R.B.;
RT "Isolation and characterization of a secreted, cell-surface glycoprotein
RT SCUBE2 from humans.";
RL Biochem. J. 422:119-128(2009).
RN [7]
RP FUNCTION, INTERACTION WITH SHH, AND SUBUNIT.
RX PubMed=22902404; DOI=10.1016/j.celrep.2012.07.010;
RA Tukachinsky H., Kuzmickas R.P., Jao C.Y., Liu J., Salic A.;
RT "Dispatched and scube mediate the efficient secretion of the cholesterol-
RT modified hedgehog ligand.";
RL Cell Rep. 2:308-320(2012).
RN [8]
RP FUNCTION, INTERACTION WITH SHH, AND SUBUNIT.
RX PubMed=22677548; DOI=10.1101/gad.191866.112;
RA Creanga A., Glenn T.D., Mann R.K., Saunders A.M., Talbot W.S., Beachy P.A.;
RT "Scube/You activity mediates release of dually lipid-modified Hedgehog
RT signal in soluble form.";
RL Genes Dev. 26:1312-1325(2012).
RN [9]
RP INTERACTION WITH SHH, FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=24522195; DOI=10.1242/jcs.137695;
RA Jakobs P., Exner S., Schuermann S., Pickhinke U., Bandari S., Ortmann C.,
RA Kupich S., Schulz P., Hansen U., Seidler D.G., Grobe K.;
RT "Scube2 enhances proteolytic Shh processing from the surface of Shh-
RT producing cells.";
RL J. Cell Sci. 127:1726-1737(2014).
RN [10]
RP FUNCTION, AND REVIEW.
RX PubMed=26875496; DOI=10.1016/j.ydbio.2016.02.009;
RA Xavier G.M., Seppala M., Barrell W., Birjandi A.A., Geoghegan F.,
RA Cobourne M.T.;
RT "Hedgehog receptor function during craniofacial development.";
RL Dev. Biol. 415:198-215(2016).
RN [11]
RP FUNCTION, AND INTERACTION WITH VEGFR2.
RX PubMed=27834687; DOI=10.1161/atvbaha.116.308546;
RA Lin Y.C., Chao T.Y., Yeh C.T., Roffler S.R., Kannagi R., Yang R.B.;
RT "Endothelial SCUBE2 interacts with VEGFR2 and regulates VEGF-induced
RT angiogenesis.";
RL Arterioscler. Thromb. Vasc. Biol. 37:144-155(2017).
RN [12]
RP INTERACTION WITH SCUBE3.
RX PubMed=33308444; DOI=10.1016/j.ajhg.2020.11.015;
RG Genomics England Research Consortium;
RA Lin Y.C., Niceta M., Muto V., Vona B., Pagnamenta A.T., Maroofian R.,
RA Beetz C., van Duyvenvoorde H., Dentici M.L., Lauffer P., Vallian S.,
RA Ciolfi A., Pizzi S., Bauer P., Gruening N.M., Bellacchio E.,
RA Del Fattore A., Petrini S., Shaheen R., Tiosano D., Halloun R.,
RA Pode-Shakked B., Albayrak H.M., Isik E., Wit J.M., Dittrich M.,
RA Freire B.L., Bertola D.R., Jorge A.A.L., Barel O., Sabir A.H.,
RA Al Tenaiji A.M.J., Taji S.M., Al-Sannaa N., Al-Abdulwahed H., Digilio M.C.,
RA Irving M., Anikster Y., Bhavani G.S.L., Girisha K.M., Haaf T., Taylor J.C.,
RA Dallapiccola B., Alkuraya F.S., Yang R.B., Tartaglia M.;
RT "SCUBE3 loss-of-function causes a recognizable recessive developmental
RT disorder due to defective bone morphogenetic protein signaling.";
RL Am. J. Hum. Genet. 108:115-133(2021).
CC -!- FUNCTION: Lipid-binding protein required for SHH long-range signaling
CC by binding to the dually lipid-modified SHH (ShhNp) and by promoting
CC ShhNp mobilization, solubilization and release from the cell membrane
CC (PubMed:22902404, PubMed:22677548). Acts by enhancing the proteolytic
CC processing (shedding) of the lipid-modified N- and C- terminal of ShhNp
CC at the cell surface (PubMed:24522195). Synergizes with DISP1 to
CC increase SHH secretion (PubMed:22902404). Probable cell surface
CC coreceptor for VEGFR2 involved in VEGFR2-mediated angiogenesis
CC (PubMed:27834687). {ECO:0000269|PubMed:22677548,
CC ECO:0000269|PubMed:22902404, ECO:0000269|PubMed:24522195,
CC ECO:0000269|PubMed:27834687, ECO:0000303|PubMed:26875496}.
CC -!- SUBUNIT: Forms homooligomers. Forms heterooligomers with SCUBE1. Forms
CC heterooligomers with SCUBE3 (PubMed:33308444). Interacts with SHH via
CC the cholesterol anchor of the dually lipid-modified SHH (ShhNp)
CC (PubMed:19480626, PubMed:22902404). Interacts with PTCH1
CC (PubMed:19480626, PubMed:22902404). Interacts with VEGFR2
CC (PubMed:27834687). {ECO:0000250|UniProtKB:Q8IX30,
CC ECO:0000269|PubMed:19480626, ECO:0000269|PubMed:22902404,
CC ECO:0000269|PubMed:27834687, ECO:0000269|PubMed:33308444}.
CC -!- SUBCELLULAR LOCATION: Secreted. Cell surface
CC {ECO:0000269|PubMed:19480626}. Note=Secreted and tethered at the cell
CC surface (PubMed:19480626). {ECO:0000269|PubMed:19480626}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NQ36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQ36-2; Sequence=VSP_021294, VSP_039955;
CC Name=3;
CC IsoId=Q9NQ36-3; Sequence=VSP_021293, VSP_021295;
CC -!- TISSUE SPECIFICITY: Expressed in a broad spectrum of adult tissues
CC (PubMed:12270931). {ECO:0000269|PubMed:12270931}.
CC -!- DOMAIN: The CUB domain is important for the interaction with the
CC cholesterol-anchor of SHH. The CUB domain regulates protease
CC recruitment and activation during SHH shedding.
CC {ECO:0000269|PubMed:24522195}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19480626}.
CC -!- CAUTION: It is unclear how SCUBE2 binds the dilipidated SHH. According
CC to a report, the SHH cholesterol-anchor, but not palmitate, seems to be
CC both necessary and sufficient for SCUBE2-mediated SHH release from the
CC cell membrane (PubMed:22902404). According to a second paper,
CC palmitoylation accelerates the rate of SCUBE2-mediated release
CC (PubMed:22677548). Cholesterol modification is sufficient for a
CC heterologous protein to bind to SCUBE2 and to be secreted in a SCUBE2-
CC dependent manner (PubMed:22902404). {ECO:0000269|PubMed:22677548,
CC ECO:0000269|PubMed:22902404}.
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DR EMBL; AJ400877; CAB92285.1; -; Genomic_DNA.
DR EMBL; AK123039; BAC85521.1; -; mRNA.
DR EMBL; AC079296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC111690; AAI11691.1; -; mRNA.
DR CCDS; CCDS53599.1; -. [Q9NQ36-3]
DR CCDS; CCDS7797.2; -. [Q9NQ36-2]
DR CCDS; CCDS81553.1; -. [Q9NQ36-1]
DR RefSeq; NP_001164161.1; NM_001170690.1. [Q9NQ36-3]
DR RefSeq; NP_001317128.1; NM_001330199.1. [Q9NQ36-1]
DR RefSeq; NP_066025.2; NM_020974.2. [Q9NQ36-2]
DR AlphaFoldDB; Q9NQ36; -.
DR BioGRID; 121754; 1.
DR STRING; 9606.ENSP00000429969; -.
DR GlyConnect; 1745; 1 N-Linked glycan (1 site).
DR GlyGen; Q9NQ36; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9NQ36; -.
DR PhosphoSitePlus; Q9NQ36; -.
DR BioMuta; SCUBE2; -.
DR DMDM; 311033510; -.
DR jPOST; Q9NQ36; -.
DR MassIVE; Q9NQ36; -.
DR PeptideAtlas; Q9NQ36; -.
DR PRIDE; Q9NQ36; -.
DR ProteomicsDB; 82071; -. [Q9NQ36-1]
DR ProteomicsDB; 82072; -. [Q9NQ36-2]
DR ProteomicsDB; 82073; -. [Q9NQ36-3]
DR Antibodypedia; 1601; 184 antibodies from 27 providers.
DR DNASU; 57758; -.
DR Ensembl; ENST00000309263.7; ENSP00000310658.3; ENSG00000175356.14. [Q9NQ36-1]
DR Ensembl; ENST00000450649.6; ENSP00000415187.2; ENSG00000175356.14. [Q9NQ36-3]
DR Ensembl; ENST00000520467.5; ENSP00000429969.1; ENSG00000175356.14. [Q9NQ36-2]
DR GeneID; 57758; -.
DR KEGG; hsa:57758; -.
DR UCSC; uc001mhj.3; human. [Q9NQ36-1]
DR CTD; 57758; -.
DR DisGeNET; 57758; -.
DR GeneCards; SCUBE2; -.
DR HGNC; HGNC:30425; SCUBE2.
DR HPA; ENSG00000175356; Tissue enhanced (epididymis).
DR MIM; 611747; gene.
DR neXtProt; NX_Q9NQ36; -.
DR OpenTargets; ENSG00000175356; -.
DR PharmGKB; PA134908812; -.
DR VEuPathDB; HostDB:ENSG00000175356; -.
DR GeneTree; ENSGT00940000153185; -.
DR HOGENOM; CLU_013079_0_0_1; -.
DR InParanoid; Q9NQ36; -.
DR OrthoDB; 73164at2759; -.
DR PhylomeDB; Q9NQ36; -.
DR TreeFam; TF351672; -.
DR PathwayCommons; Q9NQ36; -.
DR Reactome; R-HSA-5362798; Release of Hh-Np from the secreting cell.
DR BioGRID-ORCS; 57758; 10 hits in 1070 CRISPR screens.
DR ChiTaRS; SCUBE2; human.
DR GenomeRNAi; 57758; -.
DR Pharos; Q9NQ36; Tbio.
DR PRO; PR:Q9NQ36; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NQ36; protein.
DR Bgee; ENSG00000175356; Expressed in corpus epididymis and 131 other tissues.
DR ExpressionAtlas; Q9NQ36; baseline and differential.
DR Genevisible; Q9NQ36; HS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00041; CUB; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR000859; CUB_dom.
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; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF57184; SSF57184; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Developmental protein; Disulfide bond;
KW EGF-like domain; Glycoprotein; Lipid-binding; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..999
FT /note="Signal peptide, CUB and EGF-like domain-containing
FT protein 2"
FT /id="PRO_0000255580"
FT DOMAIN 45..85
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 86..127
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 128..168
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 177..213
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 217..252
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 286..321
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 323..363
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 364..402
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 403..443
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 809..921
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT REGION 847..856
FT /note="Interaction with the cholesterol-anchor of SHH"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS0"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..62
FT /evidence="ECO:0000250"
FT DISULFID 56..71
FT /evidence="ECO:0000250"
FT DISULFID 73..84
FT /evidence="ECO:0000250"
FT DISULFID 90..102
FT /evidence="ECO:0000250"
FT DISULFID 98..111
FT /evidence="ECO:0000250"
FT DISULFID 113..126
FT /evidence="ECO:0000250"
FT DISULFID 368..378
FT /evidence="ECO:0000250"
FT DISULFID 374..387
FT /evidence="ECO:0000250"
FT DISULFID 389..401
FT /evidence="ECO:0000250"
FT DISULFID 407..418
FT /evidence="ECO:0000250"
FT DISULFID 414..427
FT /evidence="ECO:0000250"
FT DISULFID 429..442
FT /evidence="ECO:0000250"
FT DISULFID 809..835
FT /evidence="ECO:0000250"
FT DISULFID 862..883
FT /evidence="ECO:0000250"
FT VAR_SEQ 444..569
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021293"
FT VAR_SEQ 482
FT /note="S -> SGLQGAYSVTCGSSSPLRNKQQKSNDSAFG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021294"
FT VAR_SEQ 639..695
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039955"
FT VAR_SEQ 806..872
FT /note="NRRCGGELGDFTGYIESPNYPGNYPANTECTWTINPPPKRRILIVVPEIFLP
FT IEDDCGDYLVMRKTS -> T (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021295"
FT VARIANT 591
FT /note="T -> M (in dbSNP:rs3751055)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_028870"
FT VARIANT 712
FT /note="Q -> H (in dbSNP:rs7395988)"
FT /id="VAR_028871"
FT VARIANT 752
FT /note="V -> G (in dbSNP:rs12419343)"
FT /id="VAR_028872"
FT VARIANT 791
FT /note="T -> S (in dbSNP:rs3751057)"
FT /id="VAR_028873"
FT VARIANT 843
FT /note="P -> R (in dbSNP:rs3751059)"
FT /id="VAR_028874"
FT CONFLICT 916
FT /note="V -> G (in Ref. 2; BAC85521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 109957 MW; 61334844A0053095 CRC64;
MGVAGRNRPG AAWAVLLLLL LLPPLLLLAG AVPPGRGRAA GPQEDVDECA QGLDDCHADA
LCQNTPTSYK CSCKPGYQGE GRQCEDIDEC GNELNGGCVH DCLNIPGNYR CTCFDGFMLA
HDGHNCLDVD ECLENNGGCQ HTCVNVMGSY ECCCKEGFFL SDNQHTCIHR SEEGLSCMNK
DHGCSHICKE APRGSVACEC RPGFELAKNQ RDCILTCNHG NGGCQHSCDD TADGPECSCH
PQYKMHTDGR SCLEREDTVL EVTESNTTSV VDGDKRVKRR LLMETCAVNN GGCDRTCKDT
STGVHCSCPV GFTLQLDGKT CKDIDECQTR NGGCDHFCKN IVGSFDCGCK KGFKLLTDEK
SCQDVDECSL DRTCDHSCIN HPGTFACACN RGYTLYGFTH CGDTNECSIN NGGCQQVCVN
TVGSYECQCH PGYKLHWNKK DCVEVKGLLP TSVSPRVSLH CGKSGGGDGC FLRCHSGIHL
SSDVTTIRTS VTFKLNEGKC SLKNAELFPE GLRPALPEKH SSVKESFRYV NLTCSSGKQV
PGAPGRPSTP KEMFITVEFE LETNQKEVTA SCDLSCIVKR TEKRLRKAIR TLRKAVHREQ
FHLQLSGMNL DVAKKPPRTS ERQAESCGVG QGHAENQCVS CRAGTYYDGA RERCILCPNG
TFQNEEGQMT CEPCPRPGNS GALKTPEAWN MSECGGLCQP GEYSADGFAP CQLCALGTFQ
PEAGRTSCFP CGGGLATKHQ GATSFQDCET RVQCSPGHFY NTTTHRCIRC PVGTYQPEFG
KNNCVSCPGN TTTDFDGSTN ITQCKNRRCG GELGDFTGYI ESPNYPGNYP ANTECTWTIN
PPPKRRILIV VPEIFLPIED DCGDYLVMRK TSSSNSVTTY ETCQTYERPI AFTSRSKKLW
IQFKSNEGNS ARGFQVPYVT YDEDYQELIE DIVRDGRLYA SENHQEILKD KKLIKALFDV
LAHPQNYFKY TAQESREMFP RSFIRLLRSK VSRFLRPYK
