GenomeNet

Database: UniProt
Entry: Q9NQ36
LinkDB: Q9NQ36
Original site: Q9NQ36 
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   13-FEB-2019, entry version 142.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=11528127;
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
RT   architecture of a conserved syntenic region on human chromosome
RT   11p15.3 (including gene 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
RP   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   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
RT   project: 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.,
RA   Mehraban F., Koemueves L.G., Tomlinson J.E., Topper J.N.;
RT   "Identification of a novel family of cell-surface proteins expressed
RT   in human vascular endothelium.";
RL   J. Biol. Chem. 277:46364-46373(2002).
RN   [6]
RP   SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH SHH AND PTCH1,
RP   FUNCTION, 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.,
RA   Hsu C.C., Yang R.B.;
RT   "Isolation and characterization of a secreted, cell-surface
RT   glycoprotein 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
RT   cholesterol-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.,
RA   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.,
RA   Ortmann C., 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).
CC   -!- FUNCTION: Lipid-binding protein required for SHH long-range
CC       signaling by binding to the dually lipid-modified SHH (ShhNp) and
CC       by promoting ShhNp mobilization, solubilization and release from
CC       the cell membrane (PubMed:22902404, PubMed:22677548). Acts by
CC       enhancing the proteolytic processing (shedding) of the lipid-
CC       modified N- and C- terminal of ShhNp at the cell surface
CC       (PubMed:24522195). Synergizes with DISP1 to increase SHH secretion
CC       (PubMed:22902404). Probable cell surface coreceptor for VEGFR2
CC       involved in VEGFR2-mediated angiogenesis (PubMed:27834687).
CC       {ECO:0000269|PubMed:22677548, ECO:0000269|PubMed:22902404,
CC       ECO:0000269|PubMed:24522195, ECO:0000269|PubMed:27834687,
CC       ECO:0000303|PubMed:26875496}.
CC   -!- SUBUNIT: Interacts with SHH via the cholesterol anchor of the
CC       dually lipid-modified SHH (ShhNp) (PubMed:19480626,
CC       PubMed:22902404). Interacts with PTCH1 (PubMed:19480626,
CC       PubMed:22902404). Forms homooligomers and heterooligomers with
CC       SCUBE1 and SCUBE3 (By similarity). Interacts with VEGFR2
CC       (PubMed:27834687). {ECO:0000250|UniProtKB:Q8IX30,
CC       ECO:0000269|PubMed:19480626, ECO:0000269|PubMed:22902404,
CC       ECO:0000269|PubMed:27834687}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Cell surface
CC       {ECO:0000269|PubMed:19480626}. Note=Secreted and tethered at the
CC       cell 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.
CC       According to a report, the SHH cholesterol-anchor, but not
CC       palmitate, seems to be both necessary and sufficient for SCUBE2-
CC       mediated SHH release from the cell membrane (PubMed:22902404).
CC       According to a second paper, palmitoylation accelerates the rate
CC       of SCUBE2-mediated release (PubMed:22677548). Cholesterol
CC       modification is sufficient for a heterologous protein to bind to
CC       SCUBE2 and to be secreted in a SCUBE2-dependent manner
CC       (PubMed:22902404). {ECO:0000269|PubMed:22677548,
CC       ECO:0000269|PubMed:22902404}.
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   UniGene; Hs.523468; -.
DR   ProteinModelPortal; Q9NQ36; -.
DR   SMR; Q9NQ36; -.
DR   BioGrid; 121754; 1.
DR   GlyConnect; 1745; -.
DR   iPTMnet; Q9NQ36; -.
DR   PhosphoSitePlus; Q9NQ36; -.
DR   BioMuta; SCUBE2; -.
DR   DMDM; 311033510; -.
DR   jPOST; Q9NQ36; -.
DR   PeptideAtlas; Q9NQ36; -.
DR   PRIDE; Q9NQ36; -.
DR   ProteomicsDB; 82071; -.
DR   ProteomicsDB; 82072; -. [Q9NQ36-2]
DR   ProteomicsDB; 82073; -. [Q9NQ36-3]
DR   DNASU; 57758; -.
DR   Ensembl; ENST00000309263; ENSP00000310658; ENSG00000175356. [Q9NQ36-1]
DR   Ensembl; ENST00000450649; ENSP00000415187; ENSG00000175356. [Q9NQ36-3]
DR   Ensembl; ENST00000520467; ENSP00000429969; ENSG00000175356. [Q9NQ36-2]
DR   GeneID; 57758; -.
DR   KEGG; hsa:57758; -.
DR   UCSC; uc001mhj.3; human. [Q9NQ36-1]
DR   CTD; 57758; -.
DR   DisGeNET; 57758; -.
DR   EuPathDB; HostDB:ENSG00000175356.12; -.
DR   GeneCards; SCUBE2; -.
DR   HGNC; HGNC:30425; SCUBE2.
DR   HPA; HPA006353; -.
DR   HPA; HPA029871; -.
DR   MIM; 611747; gene.
DR   neXtProt; NX_Q9NQ36; -.
DR   OpenTargets; ENSG00000175356; -.
DR   PharmGKB; PA134908812; -.
DR   GeneTree; ENSGT00940000153185; -.
DR   HOGENOM; HOG000230943; -.
DR   HOVERGEN; HBG054902; -.
DR   InParanoid; Q9NQ36; -.
DR   OrthoDB; 73164at2759; -.
DR   PhylomeDB; Q9NQ36; -.
DR   TreeFam; TF351672; -.
DR   Reactome; R-HSA-5362798; Release of Hh-Np from the secreting cell.
DR   ChiTaRS; SCUBE2; human.
DR   GenomeRNAi; 57758; -.
DR   PRO; PR:Q9NQ36; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000175356; Expressed in 167 organ(s), highest expression level in fundus of stomach.
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:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
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; 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; 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   SMART; SM01411; Ephrin_rec_like; 3.
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; Complete proteome;
KW   Developmental protein; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Lipid-binding; Polymorphism; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32    999       Signal peptide, CUB and EGF-like domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000255580.
FT   DOMAIN       45     85       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN       86    127       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      128    168       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      177    213       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      217    252       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      286    321       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      323    363       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      364    402       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      403    443       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      809    921       CUB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   REGION      847    856       Interaction with the cholesterol-anchor
FT                                of SHH. {ECO:0000250|UniProtKB:Q9JJS0}.
FT   CARBOHYD    659    659       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     49     62       {ECO:0000250}.
FT   DISULFID     56     71       {ECO:0000250}.
FT   DISULFID     73     84       {ECO:0000250}.
FT   DISULFID     90    102       {ECO:0000250}.
FT   DISULFID     98    111       {ECO:0000250}.
FT   DISULFID    113    126       {ECO:0000250}.
FT   DISULFID    368    378       {ECO:0000250}.
FT   DISULFID    374    387       {ECO:0000250}.
FT   DISULFID    389    401       {ECO:0000250}.
FT   DISULFID    407    418       {ECO:0000250}.
FT   DISULFID    414    427       {ECO:0000250}.
FT   DISULFID    429    442       {ECO:0000250}.
FT   DISULFID    809    835       {ECO:0000250}.
FT   DISULFID    862    883       {ECO:0000250}.
FT   VAR_SEQ     444    569       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021293.
FT   VAR_SEQ     482    482       S -> SGLQGAYSVTCGSSSPLRNKQQKSNDSAFG (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_021294.
FT   VAR_SEQ     639    695       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_039955.
FT   VAR_SEQ     806    872       NRRCGGELGDFTGYIESPNYPGNYPANTECTWTINPPPKRR
FT                                ILIVVPEIFLPIEDDCGDYLVMRKTS -> T (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021295.
FT   VARIANT     591    591       T -> M (in dbSNP:rs3751055).
FT                                {ECO:0000269|PubMed:14702039}.
FT                                /FTId=VAR_028870.
FT   VARIANT     712    712       Q -> H (in dbSNP:rs7395988).
FT                                /FTId=VAR_028871.
FT   VARIANT     752    752       V -> G (in dbSNP:rs12419343).
FT                                /FTId=VAR_028872.
FT   VARIANT     791    791       T -> S (in dbSNP:rs3751057).
FT                                /FTId=VAR_028873.
FT   VARIANT     843    843       P -> R (in dbSNP:rs3751059).
FT                                /FTId=VAR_028874.
FT   CONFLICT    916    916       V -> G (in Ref. 2; BAC85521).
FT                                {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
//
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