ID A0A1U8BQ26_MESAU Unreviewed; 1251 AA.
AC A0A1U8BQ26;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Latent-transforming growth factor beta-binding protein 3 isoform X1 {ECO:0000313|RefSeq:XP_012969327.1};
GN Name=Ltbp3 {ECO:0000313|RefSeq:XP_012969327.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012969327.1};
RN [1] {ECO:0000313|RefSeq:XP_012969327.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the LTBP family.
CC {ECO:0000256|ARBA:ARBA00038081}.
CC -!- SIMILARITY: Belongs to the fibulin family.
CC {ECO:0000256|ARBA:ARBA00006127}.
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 RefSeq; XP_012969327.1; XM_013113873.2.
DR AlphaFoldDB; A0A1U8BQ26; -.
DR GeneID; 101827539; -.
DR CTD; 4054; -.
DR OrthoDB; 354414at2759; -.
DR Proteomes; UP000189706; Unplaced.
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; 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; 9.
DR Pfam; PF12661; hEGF; 3.
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; 10.
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 3: Inferred from homology;
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 Growth factor binding {ECO:0000256|ARBA:ARBA00023183};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
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..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..1251
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010564357"
FT DOMAIN 106..138
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 274..317
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 352..392
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 400..452
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 571..612
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 613..650
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 657..694
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 741..781
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 782..822
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 823..862
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 863..905
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 914..968
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1033..1073
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1086..1132
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT REGION 243..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 110..120
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 128..137
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1251 AA; 134183 MW; C8961A901420C83D CRC64;
MPGPRGAARG LAPAMRWAGA SGLLALLLLA LLGPGGGAEG GPAGERGTGG GGALARERFK
VVFAPVICKR TCLKGQCRDS CQQGSNMTLI GENGHSTDTL TGSGFRVVVC PLPCMNGGQC
SSRNQCLCPP DFTGRFCQVP AAGTGAGTGN SGPGLARTGA MSTGPLPPLA PEGESVASKH
AIYAVQVIPD PPGPGEGPPA QHAAFLVPLG PGQISAEVQA PPPVVNVRVH HPPEASVQVH
RIDGSNTEGP ASSQHLLPHP KPPHPRPPTQ KPLGRCFQDT LPKQPCGSNP LPGLTKQEDC
CGSIGTAWGQ SKCHKCPQLQ YTGVQKPGPV RGEVGADCPQ GYKRLNSTHC QDINECAMPG
MCRHGDCLNN PGSYRCVCPS GHSLGPSRTQ CIADKPEEKS LCFRLVSTEH QCQHPLTTRL
TRQLCCCSVG KAWGARCQRC PADGTAAFKE ICPAGKGYHI LTSHQTLTIQ GESDFSLFLH
PDGPPKPQQL PESPSRAPPP EDAEEERGVT MDPPVSEERL VQQSHPTATT SPARPYPELI
SRPSPPTFHR FLPELPPSRS AVEIAPTQVT ETDECRLNQN ICGHGQCVPG PSDYSCHCNP
GYRSHPQHRY CVDVNECEAE PCGPGRGICM NTGGSYNCHC NRGYRLHVGA GGRSCVDLNE
CAKPHLCGDG GFCINFPGHY KCNCYPGYRL KTSRPPVCED IDECRDPSTC PDGKCENKPG
SYKCIACQPG YRSQGGGACR DINECSEGSP CSPGWCENLP GSFRCTCAQG YEPAPDGRSC
IDMDECEAGD VCSDGVCTNT PGSFQCQCLS GYHLSRDRSH CEDIDECDFP AACIGGDCIN
TNGSYRCLCP QGHRLVGGRK CQDIDECSQD PGLCLPHGAC ENLQGSYVCV CDEGFTLTQD
QHGCEEVEQP HHKKECYLNF DDTVFCDSVL ATNVTQQECC CSLGAGWGDH CEIYPCPVYS
SAEFHSLCPD GKGYTQDNNI VNYGIPAHRD IDECVLFGAE ICKEGKCVNT QPGYECYCKQ
GFYYDGNLLE CVDVDECLDE SNCRNGVCEN TRGGYRCACT PPAEYSPAQR QCLSPEEMEH
APERREVCWG QRGEDGMCMG PLAGPALTFD DCCCRQGRGW GTQCRPCPPQ GSQCPTSQSE
SNSFWDTSPL LLGESPRDED SSEEDSDECR CVSGRCVLRP GGAVCECPGG FQLDASRARC
VDIDECRELN QRGLLCKSER CVNTSGSFRC VCKAGFTRSR PHGACVPQRR R
//
