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Database: UniProt
Entry: TIE1_MOUSE
LinkDB: TIE1_MOUSE
Original site: TIE1_MOUSE 
ID   TIE1_MOUSE              Reviewed;        1134 AA.
AC   Q06806; Q811F4; Q8BGI2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 201.
DE   RecName: Full=Tyrosine-protein kinase receptor Tie-1;
DE            EC=2.7.10.1;
DE   Flags: Precursor;
GN   Name=Tie1; Synonyms=Tie, Tie-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/cJ; TISSUE=Lung;
RX   PubMed=8415706; DOI=10.1073/pnas.90.20.9355;
RA   Sato T.N., Qin Y., Kozak C.A., Andus K.L.;
RT   "Tie-1 and tie-2 define another class of putative receptor tyrosine kinase
RT   genes expressed in early embryonic vascular system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:9355-9358(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/cJ; TISSUE=Bone marrow;
RA   Krivsov A.V., Ershler M.A., Visser J.W.M., Belyavsky A.V.;
RL   Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ; TISSUE=Fetal liver;
RX   PubMed=8395828; DOI=10.1006/bbrc.1993.2045;
RA   Iwama A., Hamaguchi I., Hashiyama M., Murayama Y., Yasunaga K., Suda T.;
RT   "Molecular cloning and characterization of mouse TIE and TEK receptor
RT   tyrosine kinase genes and their expression in hematopoietic stem cells.";
RL   Biochem. Biophys. Res. Commun. 195:301-309(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   PubMed=7655012;
RA   Korhonen J., Lahtinen I., Halmekyto M., Alhonen L., Janne J., Dumont D.,
RA   Alitalo K.;
RT   "Endothelial-specific gene expression directed by the tie gene promoter in
RT   vivo.";
RL   Blood 86:1828-1835(1995).
RN   [8]
RP   NUCLEOTIDE SEQUENCE OF 221-352 AND 740-890.
RX   PubMed=1384789;
RA   Korhonen J., Partanen J., Armstrong E., Vaahtokari A., Elenius K.,
RA   Jalkanen M., Alitalo K.;
RT   "Enhanced expression of the tie receptor tyrosine kinase in endothelial
RT   cells during neovascularization.";
RL   Blood 80:2548-2555(1992).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [10]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=28179430; DOI=10.1161/circresaha.116.308825;
RA   Morooka N., Futaki S., Sato-Nishiuchi R., Nishino M., Totani Y.,
RA   Shimono C., Nakano I., Nakajima H., Mochizuki N., Sekiguchi K.;
RT   "Polydom Is an Extracellular Matrix Protein Involved in Lymphatic Vessel
RT   Remodeling.";
RL   Circ. Res. 120:1276-1288(2017).
CC   -!- FUNCTION: Transmembrane tyrosine-protein kinase that may modulate
CC       TEK/TIE2 activity and contribute to the regulation of angiogenesis.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBUNIT: Heterodimer with TEK/TIE2 (By similarity). Interacts with
CC       SVEP1 (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:P35590}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in developing vascular
CC       endothelial cells. Abundantly expressed in lung and heart, moderately
CC       in brain, liver and kidney, and weakly in thymus, spleen and testis.
CC       {ECO:0000269|PubMed:8395828}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in dermal lymphatic endothelial cells at
CC       16.5 and 18.5 dpc (at protein level) (PubMed:28179430). Expressed in
CC       the endocardium, dorsal aorta and maternal decidual blood vessel at 8.5
CC       dpc (PubMed:8415706). {ECO:0000269|PubMed:28179430,
CC       ECO:0000269|PubMed:8415706}.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to ANGPT1, most
CC       likely by TEK/TIE2. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Tie subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; X71425; CAA50556.1; -; mRNA.
DR   EMBL; X80764; CAA56739.1; -; mRNA.
DR   EMBL; X73960; CAA52148.1; -; mRNA.
DR   EMBL; AK052192; BAC34876.1; -; mRNA.
DR   EMBL; AK052413; BAC34979.1; -; mRNA.
DR   EMBL; AL627212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC046452; AAH46452.2; -; mRNA.
DR   EMBL; S79346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS18553.1; -.
DR   PIR; JN0711; JN0711.
DR   RefSeq; NP_035717.2; NM_011587.2.
DR   AlphaFoldDB; Q06806; -.
DR   SMR; Q06806; -.
DR   IntAct; Q06806; 1.
DR   MINT; Q06806; -.
DR   STRING; 10090.ENSMUSP00000037129; -.
DR   BindingDB; Q06806; -.
DR   ChEMBL; CHEMBL2034800; -.
DR   GlyCosmos; Q06806; 5 sites, No reported glycans.
DR   GlyGen; Q06806; 5 sites.
DR   iPTMnet; Q06806; -.
DR   PhosphoSitePlus; Q06806; -.
DR   CPTAC; non-CPTAC-3623; -.
DR   MaxQB; Q06806; -.
DR   PaxDb; 10090-ENSMUSP00000037129; -.
DR   PeptideAtlas; Q06806; -.
DR   ProteomicsDB; 259025; -.
DR   Antibodypedia; 32289; 776 antibodies from 39 providers.
DR   DNASU; 21846; -.
DR   Ensembl; ENSMUST00000047421.6; ENSMUSP00000037129.6; ENSMUSG00000033191.15.
DR   GeneID; 21846; -.
DR   KEGG; mmu:21846; -.
DR   UCSC; uc008ukh.1; mouse.
DR   AGR; MGI:99906; -.
DR   CTD; 7075; -.
DR   MGI; MGI:99906; Tie1.
DR   VEuPathDB; HostDB:ENSMUSG00000033191; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   GeneTree; ENSGT00940000157693; -.
DR   HOGENOM; CLU_008888_0_0_1; -.
DR   InParanoid; Q06806; -.
DR   OMA; AKVWWRL; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; Q06806; -.
DR   TreeFam; TF317568; -.
DR   BRENDA; 2.7.10.1; 3474.
DR   BioGRID-ORCS; 21846; 4 hits in 80 CRISPR screens.
DR   ChiTaRS; Tie1; mouse.
DR   PRO; PR:Q06806; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q06806; Protein.
DR   Bgee; ENSMUSG00000033191; Expressed in cardiac muscle of left ventricle and 198 other cell types or tissues.
DR   ExpressionAtlas; Q06806; baseline and differential.
DR   Genevisible; Q06806; MM.
DR   GO; GO:0016020; C:membrane; ISM:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0060854; P:branching involved in lymph vessel morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0060836; P:lymphatic endothelial cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IMP:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0045026; P:plasma membrane fusion; IMP:MGI.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IBA:GO_Central.
DR   GO; GO:0001936; P:regulation of endothelial cell proliferation; IMP:BHF-UCL.
DR   GO; GO:1901201; P:regulation of extracellular matrix assembly; IMP:BHF-UCL.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR   GO; GO:0048771; P:tissue remodeling; IMP:BHF-UCL.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0001570; P:vasculogenesis; ISO:MGI.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00055; EGF_Lam; 1.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd05089; PTKc_Tie1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   PANTHER; PTHR24416:SF341; TYROSINE-PROTEIN KINASE RECEPTOR TIE-1; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00047; ig; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   Angiogenesis; ATP-binding; Cell membrane; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL          1..22
FT   CHAIN           23..1134
FT                   /note="Tyrosine-protein kinase receptor Tie-1"
FT                   /id="PRO_0000024472"
FT   TOPO_DOM        23..755
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        756..780
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        781..1134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..123
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          212..254
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          256..301
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          303..343
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          349..440
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          444..543
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          546..638
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          642..736
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          835..1114
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        975
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         841..849
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         866
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         1003
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        705
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        226..235
FT                   /evidence="ECO:0000250"
FT   DISULFID        229..242
FT                   /evidence="ECO:0000250"
FT   DISULFID        244..253
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..276
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..289
FT                   /evidence="ECO:0000250"
FT   DISULFID        291..300
FT                   /evidence="ECO:0000250"
FT   DISULFID        313..325
FT                   /evidence="ECO:0000250"
FT   DISULFID        319..331
FT                   /evidence="ECO:0000250"
FT   DISULFID        333..342
FT                   /evidence="ECO:0000250"
FT   CONFLICT        307
FT                   /note="G -> D (in Ref. 1; CAA50556/CAA56739, 3; CAA52148
FT                   and 6; AAH46452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        599
FT                   /note="R -> L (in Ref. 1; CAA50556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        741
FT                   /note="G -> D (in Ref. 1; CAA50556/CAA56739, 3; CAA52148
FT                   and 6; AAH46452)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1134 AA;  124583 MW;  9669098A843B36F2 CRC64;
     MVWWGSSLLL PTLFLASHVG ASVDLTLLAN LRITDPQRFF LTCVSGEAGA GRSSDPPLLL
     EKDDRIVRTF PPGQPLYLAR NGSHQVTLRG FSKPSDLVGV FSCVGGAGAR RTRVLYVHNS
     PGAHLFPDKV THTVNKGDTA VLSAHVHKEK QTDVIWKNNG SYFNTLDWQE ADDGRFQLQL
     QNVQPPSSGI YSATYLEASP LGSAFFRLIV RGCGAGRWGP GCVKDCPGCL HGGVCHDHDG
     ECVCPPGFTG TRCEQACREG RFGQSCQEQC PGTAGCRGLT FCLPDPYGCS CGSGWRGSQC
     QEACAPGHFG ADCRLQCQCQ NGGTCDRFSG CVCPSGWHGV HCEKSDRIPQ ILSMATEVEF
     NIGTMPRINC AAAGNPFPVR GSMKLRKPDG TMLLSTKVIV EPDRTTAEFE VPSLTLGDSG
     FWECRVSTSG GQDSRRFKVN VKVPPVPLTA PRLLAKQSRQ LVVSPLVSFS GDGPISSVRL
     HYRPQDSTIA WSAIVVDPSE NVTLMNLKPK TGYNVRVQLS RPGEGGEGGW GPSALMTTDC
     PEPLLQPWLE SWHVEGPDRL RVSWSLPSVP LSGDGFLLRL WDGARGQERR ENISFPQART
     ALLTGLTPGT HYQLDVRLYH CTLLGPASPP AHVHLPPSGP PAPRHLHAQA LSDSEIQLMW
     QHPEAPSGPI SKYIVEIQVA GGSGDPQWMD VDRPEETSII VRGLNASTRY LFRVRASVQG
     LGDWSNTVEE ATLGNGLQSE GPVRESRAAE EGLDQQLVLA VVGSVSATCL TILAALLALV
     CIRRSCLHRR RTFTYQSGSG EETILQFSSG TLTLTRRPKP QPEPLSYPVL EWEDITFEDL
     IGEGNFGQVI RAMIKKDGLK MNAAIKMLKE YASENDHRDF AGELEVLCKL GHHPNIINLL
     GACENRGYLY IAIEYAPYGN LLDFLRKSRV LETDPAFARE HGTASTLSSR QLLRFASDAA
     NGMQYLSEKQ FIHRDLAARN VLVGENLASK IADFGLSRGE EVYVKKTMGR LPVRWMAIES
     LNYSVYTTKS DVWSFGVLLW EIVSLGGTPY CGMTCAELYE KLPQGYRMEQ PRNCDDEVYE
     LMRQCWRDRP YERPPFAQIA LQLGRMLEAR KAYVNMSLFE NFTYAGIDAT AEEA
//
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