ID A0A1S3GGZ2_DIPOR Unreviewed; 1309 AA.
AC A0A1S3GGZ2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Latent-transforming growth factor beta-binding protein 4 {ECO:0000313|RefSeq:XP_012888076.1};
GN Name=Ltbp4 {ECO:0000313|RefSeq:XP_012888076.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012888076.1};
RN [1] {ECO:0000313|RefSeq:XP_012888076.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012888076.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_012888076.1; XM_013032622.1.
DR STRING; 10020.ENSDORP00000018363; -.
DR GeneID; 105998026; -.
DR KEGG; dord:105998026; -.
DR CTD; 8425; -.
DR InParanoid; A0A1S3GGZ2; -.
DR OrthoDB; 354414at2759; -.
DR Proteomes; UP000081671; Unplaced.
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; 12.
DR Gene3D; 2.10.25.10; Laminin; 18.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 3.
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; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF166; VACUOLAR-SORTING RECEPTOR 1; 1.
DR Pfam; PF07645; EGF_CA; 16.
DR Pfam; PF00683; TB; 2.
DR SMART; SM00181; EGF; 18.
DR SMART; SM00179; EGF_CA; 17.
DR SUPFAM; SSF57196; EGF/Laminin; 7.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF57581; TB module/8-cys domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 12.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 13.
DR PROSITE; PS01187; EGF_CA; 7.
DR PROSITE; PS51364; TB; 3.
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:UP000081671};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1309
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010376863"
FT DOMAIN 79..111
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 217..257
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 285..321
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 335..387
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 531..569
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 573..614
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 615..652
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 654..691
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 696..737
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 778..815
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 821..862
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 863..903
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 992..1033
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1124..1178
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1196..1233
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1239..1280
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 410..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1282..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1115
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 83..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 101..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 642..651
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1309 AA; 138405 MW; CC95190B7A5BDB00 CRC64;
MAGGARLLWV SFLVLLGPQP GQGRPRERLR VRFTPAVCGL RCIHGPSGSR CTPTCAPRNA
TSVDSGAPGG AAPGGPGFRA FLCPLICHNG GVCVKPDRCL CPPDFAGKFC QLHASGARPP
APAMPGITRS VYTMPLANHR DDEHGVASMV SVHVEHPQEA SVVVHQVERV SGPWEEADPE
AVARAEAAAR AEAAAPYTVL AQSAPREDGY SDASGFGYCF RELRRGECVS PLPGLRTQEV
CCRGEGVAWG VHDCQPCSEH LGNRVGGADG PCPTGFERVN GSCVDVDECA TGGRCQHGEC
ANTRGGYTCV CPDGFLLDSS RSSCISQHVI SEAKGPCFRV LRDGGCSLPI LRNITKQICC
CSRVGKAWGR GCQLCPPFGS EGFREICPAG PGYHYSASDL RYNTRPLAQE PPRVSLSQPR
APAATSRPPT GFLPTHRPEP RPQPRPQPRP EPRPEPHPES RPESRPGPEF PLPSIPAWTG
PEIPEPGPSS GVCQRNPQVC GPGRCISRPG GHTCACDSGF RLSPQGTRCV DLDECRRVPS
PCAPGRCENT PGSFRCVCGP GFRASPRATE CLDVDECRRV PPPCDRGRCE NTPGSFLCVC
PAGYQAAPHG ASCQDVDECT QSPGLCGRGV CENLPGSFRC VCPAGFRGST CEEDVDECAQ
EPPPCGPGRC DNTAGSFHCA CPAGFRSRGP GAPCQDVDEC ARSPSPCAYG RCENTEGSFQ
CICPTGFQPN AAGSECKDVD ECENHLACPG QECVNSPGSF QCRACPAGHH LHRGRCTDVD
ECSSGAPCGL HGHCTNTEGS FRCSCAPGYR APSGRPGPCA DINECLEGDF CFPHGECLNT
DGSFACTCAP GYRPGPRGAS CLDVDECSEE DLCQSGVCTN TDGSFECICP PGHRTGPDLA
SCLDIDECRE QGSALCGSQR CENSPGSYRC VQDCDPGYHA GPEGTCDDVD ECQEYGSAIC
GAQRCENTPG SYRCVPACDP GYQPTPGGGC QDVDECRNRS FCGAHAVCQN LPGSFQCLCD
QGYEGARDGR HCVDVNECAT LQGVCGTALC ENVEGSFLCV CPSSPEEFDP MTGRCVPPRT
SAGTFPGSQP QAPASPSLPA RPPPPSAPRR PSPPRQGPVG SERRECYFDT AAPDACDNIL
ARNVTWQECC CTVGEGWGSG CRIQQCPGTE TAEYQSLCPH GRGYLASSGD LSLWRDVDEC
QLFRDQVCKS GVCVNTAPGY SCYCSNGYYY HAQRLECVDN DECADEEPAC EGGRCINTVG
SYHCTCEPPL VLDGSRRRCV SNESQSLGSP ASNPAPAVMP HPPPSLAGP
//
