ID A0A3Q7TFZ8_VULVU Unreviewed; 1817 AA.
AC A0A3Q7TFZ8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Latent-transforming growth factor beta-binding protein 2 {ECO:0000313|RefSeq:XP_025864381.1};
GN Name=LTBP2 {ECO:0000313|RefSeq:XP_025864381.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025864381.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025864381.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025864381.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025864381.1};
RG RefSeq;
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 RefSeq; XP_025864381.1; XM_026008596.1.
DR STRING; 9627.ENSVVUP00000006603; -.
DR Ensembl; ENSVVUT00000008808; ENSVVUP00000006603; ENSVVUG00000005123.
DR KEGG; vvp:112927275; -.
DR OrthoDB; 354414at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0097435; P:supramolecular fiber organization; IEA:Ensembl.
DR CDD; cd00054; EGF_CA; 13.
DR Gene3D; 2.10.25.10; Laminin; 19.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 4.
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:SF205; COMPLEMENT COMPONENT C1Q RECEPTOR; 1.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07645; EGF_CA; 16.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 20.
DR SMART; SM00179; EGF_CA; 18.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 6.
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; 8.
DR PROSITE; PS50026; EGF_3; 13.
DR PROSITE; PS01187; EGF_CA; 7.
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:UP000286640};
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..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1817
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018680124"
FT DOMAIN 187..219
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 391..423
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 544..587
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 664..716
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 840..882
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 883..919
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 926..965
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1006..1046
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1131..1171
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1172..1213
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1214..1249
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1299..1336
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1407..1459
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1481..1523
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1524..1559
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1580..1632
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1770..1814
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 76..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 191..201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 209..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 395..405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 413..422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1528..1538
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1817 AA; 195084 MW; F469ED4B3F1F1D23 CRC64;
MGPPTTHRCP GRAPRNPRGG LLALTLALFV GMGHAQRDPV GRYELAGRDA NRLRRPGGSH
PAAPAAKVYS LFREQDAPAP GLPPTERAQP GWGSPRRPAD ALARRPPRAQ QPRRAQPPAQ
TWRSSPVGQQ QSAARARVAP ALPRLGTLQR PGAAPPTPPR GRLTGRNVCG GQCCPGWTTA
NSTNHCIKPV CQPPCQNRGS CSRPQLCVCR SGFRGARCEE VIPEEEFDPQ NSRPAPRRSA
EGSPNLRRSS AARESTTTPR TRSLASQLPL VRTLSGLSQT QPSQQHMGLS RTVRLYPTTA
ANGQLTSNAL PAGPGLERRD GAQQAAYLDH PSPPWGLNLT EKIKKIKIVF TPTICKQTCA
HGHCSNSCER GDTTTLYSQG GHGHDPKSGF RIYFCQIPCL NGGRCIGRDE CWCPANSTGK
FCHLPSPKLD AGPRERGSRL GALLEGPLRQ STFTLPLSNQ LASVNPSLVK VHINHPPEAS
VQVHQVARVR GEAPEENSVE TRPSPRLPAS PRHSHWDGNS IPVRSGEAPQ PPPPIAPRPP
GRLGRCYLSS VNGQCANPLL ELTAQEDCCG SVGAFWGVTS CAPCPPRPAS PVIENGQLEC
PQGYKRLNLT HCQDINECLT LDLCKDSECV NTRGSYLCTC GPGLMLDPSR SRCVSDKAIS
MQQGLCYRSL GPGTCALPLA QSITKQICCC SRVGKAWGSK CERCPLPGTE AFREICPAGH
GYTYSSSHIR LAMRKAEEEE LARPSREQAQ KSYGTLPGPA ERQPLRAVTD TWLEAETIPD
KGDSRTGQVT TSVTQVPAWV PGDAIKRPTP PLPGQGIPDN QEEEHVTTPA EGLVALGPSG
TDRCAAGATN ICGPGTCVNL PDGYKCICNP GYQLHPSQAY CTDDNECLRD PCAGRGHCVN
RVGSYSCFCY PGYTLATSGT SQECQDVDEC EQPEVCSGGR CTNTEGSYHC QCDQGYIMVR
KGHCQDINEC RHPGTCPDGR CVNSPGSYTC LACEEGYRGQ SGSCVDVNEC LTPGVCAHGK
CINLEGSFRC SCEQGYTVTS DEKGCQDVDE CASRASCPTG LCLNTQGSFT CSACESGYWV
NEDGTACEDL DECAFPGVCP TGVCTNTAGS FSCRDCEEGY RPSPLGHTCE DVDECEDLQS
SCQGGECKNT AGSYQCLCPP GFQLANGTVC EDVDECVGEE YCAPHGECLN SHGSFFCLCA
PGFASAEGGT SCQDVDECAV TDQCLGGHCV NTEGSFNCLC ETGFQPSPES GECVDIDECK
DYGDPVCGAW RCENSPGSYR CVLGCQPGFH MAPTGDCIDI DECANDTMCG SHGFCDNTDG
SFRCLCDQGF ETSSSGWDCV DVNECELMLA VCGAALCENV EGSFLCLCAS DLEEYDAQEG
HCRPRLAAGQ SIPEAPPGDH PPGPIRMECY SGQNGQLPCS SLLGRNTTQA ECCCTQGASW
GDTCDPCPAE DSVEFSEICP SGKGYIPVDG AWMFGQTTYT DADECVMFGP GLCQNGRCLN
TVPGYICLCN AGYHYNAVHR KCEDHDECQD MACENGECVN TEGSFHCFCS PPLTLDLSQQ
RCINSTGSTE DLPDHDIHMD ICWKRVTNYV CSQPLHGRRT TYTECCCQDG EAWSQQCALC
PPRSSEVYAQ LCNVARIEAE REAGVHFRPG YEYGPGPEDL HYSLYGPDGA PFYNYLGPED
TIPEPPFPNT ASHTGDHTPV LESPLQPSEL QPHYVASQPE HQAGFEGLQA EECGILNGCE
NGRCVRVREG YTCDCFEGFQ LDMAHMACVD VNECDDLNGP AALCAHGHCE NTEGSYRCHC
SPGYVAEAGP PHCTAKE
//
