ID G1NXV0_MYOLU Unreviewed; 1629 AA.
AC G1NXV0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE SubName: Full=Latent transforming growth factor beta binding protein 1 {ECO:0000313|Ensembl:ENSMLUP00000002215.2};
GN Name=LTBP1 {ECO:0000313|Ensembl:ENSMLUP00000002215.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000002215.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000002215.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000002215.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AAPE02028510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02028511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02028512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02028513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 59463.ENSMLUP00000002215; -.
DR Ensembl; ENSMLUT00000002437.2; ENSMLUP00000002215.2; ENSMLUG00000002425.2.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000155823; -.
DR HOGENOM; CLU_001884_1_0_1; -.
DR InParanoid; G1NXV0; -.
DR OMA; SQRCTKX; -.
DR TreeFam; TF317514; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0001527; C:microfibril; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050436; F:microfibril binding; IEA:Ensembl.
DR GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; IEA:Ensembl.
DR GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 12.
DR Gene3D; 2.10.25.10; Laminin; 18.
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; 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:SF111; -; 1.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF07645; EGF_CA; 12.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 18.
DR SMART; SM00179; EGF_CA; 16.
DR SUPFAM; SSF57196; EGF/Laminin; 10.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 11.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 9.
DR PROSITE; PS50026; EGF_3; 11.
DR PROSITE; PS01187; EGF_CA; 6.
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:UP000001074};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 93..125
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 305..337
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 463..508
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 532..572
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 583..635
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 823..864
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 946..986
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 987..1027
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1028..1068
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1069..1109
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1110..1151
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1152..1189
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1255..1309
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1432..1485
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1570..1614
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 97..107
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 115..124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 309..319
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 327..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1629 AA; 177485 MW; 2FB8052FA99C7742 CRC64;
LQGLRPPPPP PPEPARPRSG GQLHPQPGGT RRAVPDRQTK AGKPRDPKVP QEEQSGGGSR
LKAQQKQQLQ GVNVCGGQCC QGWSKAPGSQ RCTKPSCVPP CQNGGMCLRP QLCVCKPGTK
GKACEMTAAQ DTSSPVFAGQ GPGAAASWVP PEQASKRTSS KKADTLPRVS PVAQMTLTLK
PKPSVGLAQQ IHSQVTPLSS QNVVIHHGQT QEYVLKPKYF AAQKVISGEQ STEGSFPLRY
GPDQVAAPFQ LSNHTGRIKV VFTPSICRVT CTKGSCQNSC EKGNTTTLIS ENGHAADTLT
ATNFRVVICH LPCMNGGQCS SRDKCQCPPN FTGKLCQIPV HGASVPKLYQ HSQQSGKALG
THVVHSTHTL PLTMTSQQGV KVKFPPNIVN IHVKHPPEAS VQIHQVSRID GPTGQKVKEA
QPGQSQISYQ GLPVQKTQTV HSTYSHQQVI PHIYPVAAKT QLGRCFQETV GSQCGKALPG
LSKQEDCCGT VGTSWGFHKC QKCPKKPSYH GYNQMMECLQ GYKRVNNTFC QDINECQLQG
VCPNGECLNT MGSYRCTCKM GFGPDPTFTT CVPDTPVISE EKGPCYRLVS SGRQCMHPLS
VHLTKQLCCC SVGKAWGPHC EKCPLPGTAA FKEICPGGMG YTVSGVHRRR PIHHHVGKGP
VFVKPKNTQP VAKSTHPPPL PAKEEPVEAL TFSREHGPGV AEPEVLVATA PPEKEIPSLD
QEKTKLEPGQ PQLSPGISTI HLHPQFPVVI EKTSPPVPVE VAPEASTSSA SQVIAPTQVT
EINECSVNPD ICGAGHCVNL PVRYTCICYE GYKFSEQQRK CTDIDECTQA PHLCSQGRCE
NTEGSFLCIC PAGFMASEEG TSCIDVDECL RPDVCGEGHC INTVGAFRCK YCDSGYRMTP
GGHCEDIDEC LSPSTCPDEQ CVNSPGSYQC VPCTEGFRGW NGQCLDVDEC LDPKVCTNGT
CSNLEGSYMC SCHKGYTPTP DHKHCKDIDE CQQGNLCMNG QCKNTEGSFR CTCGQGYQLS
AAKDQCEDID ECQHRHLCTN GQCRNTEGSF RCVCDQGYRA SALGDHCEDI NECLEDNSVC
QGGDCINTKG SYDCTCPDGF QLNDNKGCQD INECEQPGLC GPRGECLNTD GSFHCVCEQG
FTISADGRTC EDIDECVNNT VCDRHGFCDN TAGSFRCLCY QGFQAPQDGQ GCVDVNECEL
LSGVCGEAFC ENVEGSFLCV CADETQEYSP MTGQCRSRAP GDLNVEVEQS REEKKECYYN
LNDASLCDNV LAPNVTKQEC CCTSGAGWGD NCEIFPCPVL GTAEFTEMCP RGKGFVPTGE
SSYEAGDKDY KDADECLLFG QEICKNGFCL NTQPGYECYC KQGTYYDPVK LQCFDMDECQ
DPNSCIDGQC INTEGSYNCF CTHPMVLDAS EKRCVRPSES HEQIEETDVY QDLCWEHLSD
DYVCSRPLVG KQTTYTECCC LYGEAWGMQC ALCPMKDSDD YAQLCNIPVT GRRQPYGRDA
LVDFSEQYAP EADPYFIQDR FLNSFEELQA EECGILNGCE NGRCVRVQEG YTCDCFDGYH
LDMAKMTCVD VNECDELNNR MSLCKNAKCI NTEGSYKCLC LPGYVPSDKP NYCTPLNTAL
NLDKDSDLE
//