ID A0A401NKE1_SCYTO Unreviewed; 1604 AA.
AC A0A401NKE1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Latent transforming growth factor beta binding protein 2 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=scyTo_0004075 {ECO:0000313|EMBL:GCB61317.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB61317.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB61317.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB61317.1}.
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DR EMBL; BFAA01001175; GCB61317.1; -; Genomic_DNA.
DR STRING; 75743.A0A401NKE1; -.
DR OMA; YWDNYER; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
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; 11.
DR Gene3D; 2.10.25.10; Laminin; 17.
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; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF206; THROMBOMODULIN; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 13.
DR Pfam; PF00683; TB; 4.
DR SMART; SM00181; EGF; 18.
DR SMART; SM00179; EGF_CA; 16.
DR SUPFAM; SSF57196; EGF/Laminin; 7.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 9.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 11.
DR PROSITE; PS01187; EGF_CA; 6.
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:UP000288216};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..30
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 212..244
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 355..397
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 425..461
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 475..527
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 690..731
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 732..768
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 812..852
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 895..936
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 937..979
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 980..1020
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1065..1103
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1178..1232
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT DOMAIN 1298..1338
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1355..1408
FT /note="TB"
FT /evidence="ECO:0000259|PROSITE:PS51364"
FT REGION 70..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 2..12
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 20..29
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 216..226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 234..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GCB61317.1"
SQ SEQUENCE 1604 AA; 175952 MW; 714C7DB022293AD8 CRC64;
VCDPPCQNRG SCSRPQLCVC RSGFQGSRCE EIVPEQPYIP RAFSSRSFSS RSSALHSNIF
PRIESSAKNN TKITSEASAR HKASPVGQSF VTQHRHGQHG STQQSSGTSR TVKHLSNGNG
QLLSNALFNG NGQTSVQNHY TTNGQVLAEN KNALPRGGNL TTSIGTIKIV FTPTICKRQC
INGKCYNNCK KGDPTTLYSE NGYGPVSKSG FRIYFCQIPC LNGGYCIGRD KCRCPSNSTG
KFCHLPVPPE KQTVSKTIPV RSSGSQSVYT LPLSNQQVLM LPSLVNIHVN HPPEATVQIH
QVARVKNAPD ASTTNSIKIS QGQQSAHSVQ QRSQLNADGN INGQPQPQHR PMNVGRCFQE
TADGQCGKPL PGLTKQDDCC GSVGISWGYH KCTKCPPTPE HPKIHNGQVE CPLGYKKMNQ
TSCKDINECL MSGMCQNANC LNTRGSYRCT CKPGYMLDTS RSHCISDKAV SVEKGTCFRS
LSRRNCSLPL SQQITKQICC CSRVGKGWGR NCEKCPLPGS VVFNEICPAG HGYHYSRSHI
QISVRPAEEH ELAQITSESE QYLDSQQSTI KDSDLTSKEK NEDVRLEGYD TTIKAPQQPQ
PFAPAHVPRI DAYPVEVVVK TSPPTLVHVV PESTARQVAS VFATEISVIN VCDVSPNICG
PGLCINQQVG YLCKCDSGYQ LDNQQTKCVD TNECREVPQL CSYGQCENTV GGYQCICSTG
FMLNQQGTDC TDINECAQAH LCRRGHCTNT PGSYRCDCEV GYMMTRSGQC NDIDECRSPN
TCPTGECINT MGSFECVSCS TGYIAINGRC RDENECLSFG ICANGNCINT DGSYKCICNQ
GFEPVTDLKS CRDIDECVSP DVCFNGLCTN TEGSYTCSSC NSGYRVSEDR DRCEDMNECL
SKGICGPNGE CMNVEGSYFC ICARGFENTP DGTGCQDINE CLARDICGPN GECINNEAGS
YYCLCAQGYT TTADGTGCED VNECSEEAKC SGGQCINTDG SYMCRCETGF THLPEAEQCL
DIDECSLYDS SVCGTWKCEN TVGSYQCIVG CQPGFQRTAI GECIDIDECI NGTICGTHGY
CENTDGSFRC HCDQGFEVPP RGQGCVDIDE CEMMNGVCGT ALCENFEGSF FCECMDENED
FDPARGQCRP RIAMEDTPGV SIVPELPRMS APAKGDLKEC YYNLNDENFC DNLLSRNITK
EECCCTVGVG WGDNCEVHPC PIINTDEYNE ICPDGKGFIP FQIGSFSFGS QNYGDADECA
MFGSEICKNG HCVNNIGDYA CYCGTGFYYD NVRLECVDID ECQDENTCVN GECVNTPGAF
NCFCSPPLTL DVTRKRCING TESGVDSEEV DTYLDICWQG VTEDDICSKP LRTRSTTYTE
CCCLYGEAWG LQCAFCPSRT SDDFAQLCNI PRIFGDVSTG LHDRPGYEYG PETPSFGQDF
QRGIGSYDNY LQPEYRPYDS QRELEYGPVD PYLGPRFEPR DPQPGSVYEL RDPHLTPQYG
LTDPRFGEGY GSRNPQPRPE YGSRGDSHTE QYRPREPGRV PLFSSSDNDR SSSFEGLQAE
ECGILNGCEN GRCVRVEEGY TCDCFDGFEL DMTKMTCILM NVRI
//
