ID G3SA40_GORGO Unreviewed; 1285 AA.
AC G3SA40;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Latent transforming growth factor beta binding protein 3 {ECO:0000313|Ensembl:ENSGGOP00000024961.2};
GN Name=LTBP3 {ECO:0000313|Ensembl:ENSGGOP00000024961.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000024961.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000024961.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000024961.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000024961.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; CABD030079744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030079745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9593.ENSGGOP00000024961; -.
DR Ensembl; ENSGGOT00000029544.2; ENSGGOP00000024961.2; ENSGGOG00000000714.3.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000160285; -.
DR HOGENOM; CLU_001884_1_0_1; -.
DR InParanoid; G3SA40; -.
DR OMA; CRDSCHH; -.
DR TreeFam; TF317514; -.
DR Proteomes; UP000001519; Chromosome 11.
DR Bgee; ENSGGOG00000000714; Expressed in heart and 5 other cell types or tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0060430; P:lung saccule development; IEA:Ensembl.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; IEA:Ensembl.
DR GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; IEA:Ensembl.
DR GO; GO:0036363; P:transforming growth factor beta activation; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 10.
DR Gene3D; 2.10.25.10; Laminin; 15.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 4.
DR InterPro; IPR026823; cEGF.
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 PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF166; VACUOLAR-SORTING RECEPTOR 1; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 10.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 14.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 9.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 11.
DR PROSITE; PS01187; EGF_CA; 6.
DR PROSITE; PS51364; TB; 4.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1285
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014167415"
FT DOMAIN 91..123
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 259..302
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 337..377
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 385..437
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 556..597
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 598..635
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 642..684
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 726..766
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 767..807
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 808..847
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 848..890
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 899..953
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1018..1058
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1064..1104
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1118..1163
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT REGION 231..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 95..105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 113..122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1285 AA; 137517 MW; 08533525E98F71FB CRC64;
RGAGAAGLLA LLLLLLLGLG GRVEGGPAGE RGAGGGGALA RERFKVVFAP VICKRTCLKG
QCRDSCQQGS NMTLIGENGH STDTLTGSGF RVVVCPLPCM NGGQCSSRNQ CLCPPDFTGR
FCQVPAGGAG GGTGGSGPGL SRAGALSTGA LPPLAPEGDS VASKHAIYAV QVIADPPGPG
EGPPAQHAAF LVPLGPGQIS AEVQAPPPVV NVRVHHPPEA SVQVHRIESS NAEGAAPSQH
LLPHPKPSHP RPPTQKPLGR CFQDTLPKQP CGSNPLPGLT KQEDCCGSIG TAWGQSKCHK
CPQLQYTGVQ KPGPVRGEVG ADCPQGYKRL NSTHCQDINE CAMPGVCRHG DCLNNPGSYR
CVCPPGHSLG PSRTQCIADK PEEKSLCFRL VSPEHQCQHP LTTRLTRQLC CCSVGKAWGA
RCQRCPTDGT AAFKEICPAG KGYHILTSHQ TLTIQGESDF SLFLHPDGPP KPQQLPESPS
QAPPPEDTEE ERGVTTDSPV SEERSVQQSH PTATTTPARP YPELISRPSP PTMRWFLPDL
PPSRSAVEIA PTQVTETDEC RLNQNICGHG ECVPGPPDYS CHCNPGYRSH PQHRYCVDVN
ECEAEPCGPG RGICMNTGGS YNCHCNRGYR LHVGAGGRSC VDLNECAKPH LCGDGGFCIN
FPGHYKCNCY PGYRLKASRP PVCEDIDECR DPSSCPDGKC ENKPGSFKCI ACQPGYRSQG
GGACRDVNEC AEGSPCSPGW CENLPGSFRC TCAQGYAPAP DGRSCLDVDE CEAGDVCDNG
ICSNTPGSFQ CQCLSGYHLS RDRSHCEDID ECDFPAACIG GDCINTNGSY RCLCPQGHRL
VGGRKCQDID ECSQDPGLCL PHGACKNLQG SYVCVCDEGF TPTQDQHGCE EVEQPHHKKE
CYLNFDDTVF CDSVLATNVT QQECCCSLGA GWGDHCEIYP CPVYSSAEFH SLCPDGKGYT
QDNNIVNYGI PAHRDIDECM LFGSEICKEG KCVNTQPGYE CYCKQGFYYD GNLLECVDVD
ECLDESNCRN GVCENTRGGY RCACTPPAEY SPAQRQCLSP EEMDVDECQD PAACRPGRCV
NLPGSYRCEC RPPWVPGPSG RDCQLSESPA ERAPERRDVC WSQRGEDGMC AGPLAGPALT
FDDCCCRQGR GWGAQCRPCP PRGAGSQCPT SQSESNSFWD TSPLLLGKPP RDEDSSEEDS
DECRCVSGRC VPRPGGAVCE CPGGFQLDAS RARCVDIDEC RELNQRGLLC KSERCVNTSG
SFRCVCKAGF ARSRPHGACV PQRRR
//
