GenomeNet

Database: UniProt
Entry: Q61810
LinkDB: Q61810
Original site: Q61810 
ID   LTBP3_MOUSE             Reviewed;        1253 AA.
AC   Q61810; F8VQ06; Q8BNQ6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 4.
DT   10-APR-2019, entry version 156.
DE   RecName: Full=Latent-transforming growth factor beta-binding protein 3;
DE            Short=LTBP-3;
DE   Flags: Precursor;
GN   Name=Ltbp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RX   PubMed=7730318; DOI=10.1074/jbc.270.17.10147;
RA   Yin W., Smiley E., Germiller J., Mecham R.P., Florer J.B.,
RA   Wenstrup R.J., Bonadio J.;
RT   "Isolation of a novel latent transforming growth factor-beta binding
RT   protein gene (LTBP-3).";
RL   J. Biol. Chem. 270:10147-10160(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   INTERACTION WITH TGFB1.
RX   PubMed=9602168; DOI=10.1016/S0167-4838(98)00003-X;
RA   Yin W., Fang J., Smiley E., Bonadio J.;
RT   "8-cysteine TGF-BP structural motifs are the site of covalent binding
RT   between mouse LTBP-3, LTBP-2, and latent TGF-beta 1.";
RL   Biochim. Biophys. Acta 1383:340-350(1998).
RN   [5]
RP   INTERACTION WITH TGFB1.
RX   PubMed=12062452; DOI=10.1016/S0014-5793(02)02648-0;
RA   Chen Y., Dabovic B., Annes J.P., Rifkin D.B.;
RT   "Latent TGF-beta binding protein-3 (LTBP-3) requires binding to TGF-
RT   beta for secretion.";
RL   FEBS Lett. 517:277-280(2002).
RN   [6]
RP   REVIEW.
RX   PubMed=10743502; DOI=10.1016/S1359-6101(99)00010-6;
RA   Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.;
RT   "Latent transforming growth factor-beta binding proteins (LTBPs)
RT   -- structural extracellular matrix proteins for targeting TGF-beta
RT   action.";
RL   Cytokine Growth Factor Rev. 10:99-117(1999).
RN   [7]
RP   REVIEW.
RX   PubMed=11104663; DOI=10.1042/bj3520601;
RA   Oklu R., Hesketh R.;
RT   "The latent transforming growth factor beta binding protein (LTBP)
RT   family.";
RL   Biochem. J. 352:601-610(2000).
CC   -!- FUNCTION: Key regulator of transforming growth factor beta (TGFB1,
CC       TGFB2 and TGFB3) that controls TGF-beta activation by maintaining
CC       it in a latent state during storage in extracellular space.
CC       Associates specifically via disulfide bonds with the Latency-
CC       associated peptide (LAP), which is the regulatory chain of TGF-
CC       beta, and regulates integrin-dependent activation of TGF-beta.
CC       {ECO:0000303|PubMed:10743502, ECO:0000303|PubMed:11104663}.
CC   -!- SUBUNIT: Forms part of the large latent transforming growth factor
CC       beta (TGFB1) precursor complex; removal is essential for
CC       activation of complex. {ECO:0000269|PubMed:12062452,
CC       ECO:0000269|PubMed:9602168}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9NS15}.
CC       Secreted, extracellular space, extracellular matrix
CC       {ECO:0000250|UniProtKB:Q9NS15}. Note=Secretion occurs after
CC       coexpression with TGFB1 and requires complexing with 'Cys-33' of
CC       the TGFB1 propeptide. {ECO:0000250|UniProtKB:Q9NS15}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61810-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61810-2; Sequence=VSP_009242, VSP_009243;
CC   -!- DEVELOPMENTAL STAGE: At 8.5-9.0 dpc highly expressed in liver.
CC       Significant expression was also seen in the developing central
CC       nervous, somites and cardiovascular tissue. At 13.5-16.5 dpc
CC       expression was seen in osteoblasts, respiratory epithelial cells,
CC       and nephrons and dermal connective tissue.
CC       {ECO:0000269|PubMed:7730318}.
CC   -!- PTM: Contains hydroxylated asparagine residues.
CC       {ECO:0000250|UniProtKB:Q14766}.
CC   -!- PTM: Two intrachain disulfide bonds from the TB3 domain are
CC       rearranged upon TGFB1 binding, and form interchain bonds with
CC       TGFB1 propeptide, anchoring it to the extracellular matrix.
CC       {ECO:0000250|UniProtKB:Q14766}.
CC   -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB53015.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAB53015.1; Type=Frameshift; Positions=6, 38, 56, 155, 158, 160, 481, 777; Evidence={ECO:0000305};
DR   EMBL; L40459; AAB53015.1; ALT_SEQ; mRNA.
DR   EMBL; AK080869; BAC38053.1; -; mRNA.
DR   EMBL; AC134563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A57293; A57293.
DR   RefSeq; NP_032546.2; NM_008520.2. [Q61810-1]
DR   UniGene; Mm.182396; -.
DR   ProteinModelPortal; Q61810; -.
DR   SMR; Q61810; -.
DR   BioGrid; 201221; 1.
DR   DIP; DIP-48641N; -.
DR   IntAct; Q61810; 2.
DR   STRING; 10090.ENSMUSP00000080214; -.
DR   CarbonylDB; Q61810; -.
DR   iPTMnet; Q61810; -.
DR   PhosphoSitePlus; Q61810; -.
DR   jPOST; Q61810; -.
DR   PaxDb; Q61810; -.
DR   PeptideAtlas; Q61810; -.
DR   PRIDE; Q61810; -.
DR   DNASU; 16998; -.
DR   Ensembl; ENSMUST00000081496; ENSMUSP00000080214; ENSMUSG00000024940. [Q61810-1]
DR   GeneID; 16998; -.
DR   KEGG; mmu:16998; -.
DR   CTD; 4054; -.
DR   MGI; MGI:1101355; Ltbp3.
DR   eggNOG; ENOG410IR6V; Eukaryota.
DR   eggNOG; ENOG4110G15; LUCA.
DR   GeneTree; ENSGT00940000160285; -.
DR   HOGENOM; HOG000293153; -.
DR   HOVERGEN; HBG052370; -.
DR   InParanoid; Q61810; -.
DR   KO; K08023; -.
DR   OMA; PKPQHPR; -.
DR   OrthoDB; 1174178at2759; -.
DR   PhylomeDB; Q61810; -.
DR   TreeFam; TF317514; -.
DR   Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR   ChiTaRS; Ltbp3; mouse.
DR   PRO; PR:Q61810; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000024940; Expressed in 315 organ(s), highest expression level in ciliary body.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; ISA:MGI.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
DR   GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR   GO; GO:0046849; P:bone remodeling; IMP:MGI.
DR   GO; GO:0060430; P:lung saccule development; IMP:MGI.
DR   GO; GO:0030502; P:negative regulation of bone mineralization; IMP:MGI.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:MGI.
DR   GO; GO:0045780; P:positive regulation of bone resorption; IMP:MGI.
DR   GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; ISO:MGI.
DR   GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; ISO:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   GO; GO:0036363; P:transforming growth factor beta activation; ISO:MGI.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR   Gene3D; 3.90.290.10; -; 4.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR017878; TB_dom.
DR   InterPro; IPR036773; TB_dom_sf.
DR   Pfam; PF07645; EGF_CA; 11.
DR   Pfam; PF00683; TB; 4.
DR   SMART; SM00181; EGF; 14.
DR   SMART; SM00179; EGF_CA; 13.
DR   SUPFAM; SSF57184; SSF57184; 3.
DR   SUPFAM; SSF57581; SSF57581; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 10.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 12.
DR   PROSITE; PS01187; EGF_CA; 11.
DR   PROSITE; PS51364; TB; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Growth factor binding; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     38       {ECO:0000255}.
FT   CHAIN        39   1253       Latent-transforming growth factor beta-
FT                                binding protein 3.
FT                                /FTId=PRO_0000007647.
FT   DOMAIN      106    138       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      274    328       TB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN      352    392       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      400    452       TB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN      571    612       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      613    656       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      657    699       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      741    781       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      782    822       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      823    861       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      863    905       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      914    968       TB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN      990   1032       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1033   1072       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1086   1136       TB 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN     1204   1231       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   COMPBIAS     21     32       Poly-Leu.
FT   COMPBIAS     47     52       Poly-Gly.
FT   COMPBIAS    191    292       Pro-rich.
FT   COMPBIAS    481    557       Pro-rich.
FT   COMPBIAS    575    891       Cys-rich.
FT   CARBOHYD     86     86       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    346    346       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    842    842       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    933    933       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1225   1225       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    110    120       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    114    126       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    128    137       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    276    300       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    286    313       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    301    316       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    356    367       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    362    376       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    378    391       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    402    425       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    412    437       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    426    440       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    427    452       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    575    587       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    582    596       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    598    611       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    617    629       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    622    638       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    661    673       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    667    682       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    684    698       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    745    756       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    751    765       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    767    780       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    786    797       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    792    806       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    808    821       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    827    838       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    833    847       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    849    861       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    867    880       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    874    889       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    891    904       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    916    939       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    926    951       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    926    926       Interchain (with C-33 in TGFB1); in
FT                                linked form.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   DISULFID    940    956       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    941    968       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    951    951       Interchain (with C-33 in TGFB1); in
FT                                linked form.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   DISULFID    994   1007       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1002   1016       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1018   1031       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1037   1048       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1043   1057       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1059   1072       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1113   1127       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1114   1136       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1208   1223       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1218   1232       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     863    884       DIDECSQDPGLCLPHGACENLQ -> GMRSWPGILKGEAGQ
FT                                CDLFDTL (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_009242.
FT   VAR_SEQ     885   1253       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_009243.
FT   CONFLICT     16     16       R -> H (in Ref. 2; BAC38053).
FT                                {ECO:0000305}.
FT   CONFLICT     20     20       A -> G (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT     35     35       Missing (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT     45     45       E -> Q (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT    104    104       G -> A (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT    172    172       E -> Q (in Ref. 2; BAC38053).
FT                                {ECO:0000305}.
FT   CONFLICT    263    263       Q -> P (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT    328    328       G -> V (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT    361    363       MCR -> NVC (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT    387    389       SRT -> LAA (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT    454    454       Missing (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT    662    662       T -> A (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
FT   CONFLICT    851    851       Q -> L (in Ref. 1; AAB53015).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1253 AA;  134363 MW;  C773F38FD65F186E CRC64;
     MPGPRGAAHG LAPAMRQAGA LGLLALLLLA LLGPGGGAEG GPAGERGTGG GGALARERFK
     VVFAPVICKR TCLKGQCRDS CQQGSNMTLI GENGHSTDTL TGSGFRVVVC PLPCMNGGQC
     SSRNQCLCPP DFTGRFCQVP AAGTGAGTGS SGPGLARTGA MSTGPLPPLA PEGESVASKH
     AIYAVQVIAD PPGPGEGPPA QHAAFLVPLG PGQISAEVQA PPPVVNVRVH HPPEASVQVH
     RIEGPNAEGP ASSQHLLPHP KPQHPRPPTQ KPLGRCFQDT LPKQPCGSNP LPGLTKQEDC
     CGSIGTAWGQ SKCHKCPQLQ YTGVQKPGPV RGEVGADCPQ GYKRLNSTHC QDINECAMPG
     MCRHGDCLNN PGSYRCVCPP GHSLGPSRTQ CIADKPEEKS LCFRLVSTEH QCQHPLTTRL
     TRQLCCCSVG KAWGARCQRC PADGTAAFKE ICPAGKGYHI LTSHQTLTIQ GESDFSLFLH
     PDGPPKPQQL PESPSRAPPL EDTEEERGVT MDPPVSEERS VQQSHPTTTT SPPRPYPELI
     SRPSPPTFHR FLPDLPPSRS AVEIAPTQVT ETDECRLNQN ICGHGQCVPG PSDYSCHCNA
     GYRSHPQHRY CVDVNECEAE PCGPGKGICM NTGGSYNCHC NRGYRLHVGA GGRSCVDLNE
     CTKPHLCGDG GFCINFPGHY KCNCYPGYRL KASRPPICED IDECRDPSTC PDGKCENKPG
     SFKCIACQPG YRSQGGGACR DVNECSEGTP CSPGWCENLP GSYRCTCAQG YEPAQDGLSC
     IDVDECEAGK VCQDGICTNT PGSFQCQCLS GYHLSRDRSR CEDIDECDFP AACIGGDCIN
     TNGSYRCLCP QGHRLVGGRK CQDIDECSQD PGLCLPHGAC ENLQGSYVCV CDEGFTLTQD
     QHGCEEVEQP HHKKECYLNF DDTVFCDSVL ATNVTQQECC CSLGAGWGDH CEIYPCPVYS
     SAEFHSLCPD GKGYTQDNNI VNYGIPAHRD IDECILFGAE ICKEGKCVNT QPGYECYCKQ
     GFYYDGNLLE CVDVDECLDE SNCRNGVCEN TRGGYRCACT PPAEYSPAQR QCLSPEEMEH
     APERREVCWG QRGEDGMCMG PLAGPALTFD DCCCRQGRGW GTQCRPCPPR GTGSQCPTSQ
     SESNSFWDTS PLLLGKSPRD EDSSEEDSDE CRCVSGRCVP RPGGAVCECP GGFQLDASRA
     RCVDIDECRE LNQRGLLCKS ERCVNTSGSF RCVCKAGFTR SRPHGACVPQ RRR
//
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