ID A0A2I3RAU4_PANTR Unreviewed; 1240 AA.
AC A0A2I3RAU4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Latent transforming growth factor beta binding protein 3 {ECO:0000313|Ensembl:ENSPTRP00000061743.1};
GN Name=LTBP3 {ECO:0000313|Ensembl:ENSPTRP00000061743.1,
GN ECO:0000313|VGNC:VGNC:1094};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000061743.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000061743.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000061743.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACZ04016219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3RAU4; -.
DR Ensembl; ENSPTRT00000082769.1; ENSPTRP00000061743.1; ENSPTRG00000003880.6.
DR VGNC; VGNC:1094; LTBP3.
DR GeneTree; ENSGT00940000160285; -.
DR Proteomes; UP000002277; Chromosome 11.
DR Bgee; ENSPTRG00000003880; Expressed in cerebellar cortex and 20 other cell types or tissues.
DR GO; GO:0031012; C:extracellular matrix; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 10.
DR Gene3D; 2.10.25.10; Laminin; 14.
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; PTHR24040:SF13; FIBROPELLIN-1; 1.
DR PANTHER; PTHR24040; LAMININ G-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 9.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00179; EGF_CA; 13.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 8.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 10.
DR PROSITE; PS01187; EGF_CA; 5.
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:UP000002277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..1240
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014143619"
FT DOMAIN 103..135
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 265..308
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 343..383
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 391..443
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 558..599
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 600..637
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 644..686
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 728..768
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 769..809
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 810..849
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 850..892
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 901..955
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1020..1060
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1073..1123
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT REGION 237..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 107..117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 125..134
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1240 AA; 132869 MW; 52F74516474280D7 CRC64;
MPGPRGAAGG LAPEMRGAGA AGLLALLLLG LGGRVEGGPA GERGAGGGGA LARERFKVVF
APVICKRTCL KGQCRDSCQQ GSNMTLIGEN GHSTDTLTGS GFRVVVCPLP CMNGGQCSSR
NQCLCPPDFT GRFCQVPAGG AGGGTGASGP GLSRAGALST GALPPLAPEG DSVASKHHAA
FLVPLEGTRQ LANPGRSPVA LRPLRPPPVQ APPPVVNVRV HHPPEASVQV HRIESSNAEG
AAPSQHLLPH PKPSHPRPPT QKPLGRCFQD TLPKQPCGSN PLPGLTKQED CCGSIGTAWG
QSKCHKCPQL QYTGVQKPGP VRGEVGADCP QGYKRLNSTH CQDINECAMP GVCRHGDCLN
NPGSYRCVCP PGHSLGPSRT QCIADKPEEK SLCFRLVSPE HQCQHPLTTR LTRQLCCCSV
GKAWGARCQR CPTDGTAAFK EICPAGKGYH ILTSHQTLTI QGESDFSLFL HPDGPPKPQQ
LPESPSQAPP PEDTEEERGL PVSEERSVQQ SHPTATTTPA RPYPELISRP SPPTMRWFLP
DLPPSRSAVE IAPTQVTETD ECRLNQNICG HGECVPGPPD YSCHCNPGYR SHPQHRYCVD
VNECEAEPCG PGRGICMNTG GSYNCHCNRG YRLHVGAGGR SCVDLNECAK PHLCGDGGFC
INFPGHYKCN CYPGYRLKAS RPPVCEDIDE CRDPSSCPDG KCENKPGSFK CIACQPGYRS
QGGGACRDVN ECAEGSPCSP GWCENLPGSF RCTCAQGYAP APDGRSCLDV DECEAGDVCD
NGICSNTPGS FQCQCLSGYH LSRDRSHCED IDECDFPAAC IGGDCINTNG SYRCLCPQGH
RLVGGRKCQD IDECSQDPSL CLPHGACKNL QGSYVCVCDE GFTPTQDQHG CEEVEQPHHK
KECYLNFDDT VFCDSVLATN VTQQECCCSL GAGWGDHCEI YPCPVYSSAE FHSLCPDGKG
YTQDNNIVNY GIPAHRDIDE CMLFGSEICK EGKCVNTQPG YECYCKQGFY YDGNLLECVD
VDECLDESNC RNGVCENTRG GYRCACTPPA EYSPAQRQCL SPEEMERAPE RRDVCWSQRG
EDGMCAGPLA GPALTFDDCC CRQGRGWGAQ CRPCPPRGAG SHCPTSQSES NSFWDTSPLL
LGKPPRDEDS SEEDSDECRC VSGRCVPRPG GAVCECPGGF QLDASRARCV DIDECRELNQ
RGLLCKSERC VNTSGSFRCV CKAGFARSRP HGACVPQRRR
//