ID A0A2P4T9H9_BAMTH Unreviewed; 2710 AA.
AC A0A2P4T9H9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 3 {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=CIB84_003234 {ECO:0000313|EMBL:POI33014.1};
OS Bambusicola thoracicus (Chinese bamboo-partridge) (Perdix thoracica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Bambusicola.
OX NCBI_TaxID=9083 {ECO:0000313|EMBL:POI33014.1, ECO:0000313|Proteomes:UP000237246};
RN [1] {ECO:0000313|EMBL:POI33014.1, ECO:0000313|Proteomes:UP000237246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RTK389 {ECO:0000313|EMBL:POI33014.1};
RC TISSUE=Blood {ECO:0000313|EMBL:POI33014.1};
RA Tiley G.P., Kimball R.T., Braun E.L., Burleigh J.G.;
RT "Comparison of the Chinese Bamboo Partridge and Red Junglefowl genome
RT sequences highlights the importance of demography in genome evolution.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor that may have an important role in cell/cell
CC signaling during nervous system formation.
CC {ECO:0000256|ARBA:ARBA00002066}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily.
CC {ECO:0000256|ARBA:ARBA00007343}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000256|ARBA:ARBA00010933}.
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:POI33014.1}.
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DR EMBL; PPHD01004407; POI33014.1; -; Genomic_DNA.
DR Proteomes; UP000237246; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 4.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 7.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR NCBIfam; TIGR00815; sulP; 1.
DR PANTHER; PTHR11814:SF113; SOLUTE CARRIER FAMILY 26 MEMBER 6; 1.
DR PANTHER; PTHR11814; SULFATE TRANSPORTER; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF01740; STAS; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000237246};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1313..1336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1348..1366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1372..1394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1415..1434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2003..2028
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2083..2110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2178..2197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2209..2226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2254..2282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2294..2318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2330..2347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2391..2420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..205
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 207..243
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 247..285
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 286..490
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 493..529
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 535..712
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 714..750
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 751..788
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 845..892
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 877..950
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 1311..1468
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DOMAIN 2444..2626
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT REGION 1617..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1916..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2497..2518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1868..1882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1926..1947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 195..204
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 233..242
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 519..528
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 740..749
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 778..787
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 845..857
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 847..864
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 866..875
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT NON_TER 2710
FT /evidence="ECO:0000313|EMBL:POI33014.1"
SQ SEQUENCE 2710 AA; 297475 MW; D1967117817FE886 CRC64;
MVSKENKDER ELNKQEMGLE KKGCGADDGI HSVTAQCVLR VIIITEDMLA NSITVRLENM
WQERFLSPLL ATFLEGVATV LATPKEDVFI FNIQNDTDVG GTVLNVSFSA LAPRGGHYFS
SEELQEQLYM KRMALTGASM LEVLPFDDNV CLREPCQNYM KCISVLKFDS SAPFIASPST
LFRPIHPITG LRCRCPQGFT GDYCETEINL CYSNPCLHGG TCTRKEGGYT CVCRQHFSGE
NCEVDSRSGR CQPGVCRNGG TCTNGADGGF RCQCPAGGFE TPFCELSTRS FPPRSFVMFR
GLRQRFHLTL SLSFSTVEPG GLLLYNGRLN ERHDFLAVEI IQGQVQLKYS TGESSTVVSP
YLPGGVSDGQ WHTLQLRYYN KPKVSALGVV QGPSKDKVAI LTVDECDASV ALQFGSEIGN
YSCAAEGVQT SSKKSLDLTG PLLLGGVPNL PENFPVSHRD FVGCMRDLYI DNKRIDLASY
IANNGTTAGC HAKHSFCDSS PCKNGGTCSV SWGTYSCLCP VGFGGKDCRH AMHHAHYFQG
NSVLSWDFKA DMKISVPWYL GLAFRTRQMD GVLLQAHAGQ YTTLLCQLSG GLLSFMVSRG
SGRSTSLVLD QLQLNDGRWH DLQLELRDVR SGRDSRYVIT IMLDFGLYQD TVVVGNELHG
LKVKHLHVGG VLGSGEVQNG LRGCIQGVRL GDSVTGTVLP KPSHALRVEA GCSVPSPCDS
SPCPANSICK DEWQSYSCVC QPGYYGGECV DACHLNPCKN KSVCRRKPGS PLGYVCECGG
NFFGQYCEHR MDQQCPKGWW GNPSCGPCNC DVSKGFDPDC NKTNGQCHCK DFHYRPKGSD
TCLPCDCYPV GSSSRSCDKE TGRCHCRPGV IGRQCNSCDS PFAEVTPSGC KVLYDGCPKS
LKAGVWWPQT KFGFSAVVLC PKGSLGAAVR HCDEEKGWLE PDLFNCTSPA FKELSMLLEG
LERNETELNT IEAKKLAHRL RAVTDHMDHY FGNDVHITYR LLSRLMAFES QQHGFGLTAT
QDAHFNENLL RAGSSVLAPE NREHWAMLPH SEHGSASLME QLRDYSGTLA SNMKLTYLNP
VGVVTPNIML SIDRMENHSH IRRRYPRYHS SLFRGQPAWD PHTHVVLPLS VLSPPKAEAV
PTAVPTVAGG EGNYTVESSS PRQALPEPEP ALTVIILIMY RTLGGLLPAR YQVDRRSVRY
VLLFTLHEQW WKEAGWTLAT TDNHTFLRGP LDTPLVLEFR LLETANRSKP LCVQWNHSSP
TNPSGFWTAK DCDLVYRNTT HVHCQCSQFG TFGVLMDSSH REQLEGDLET LAIVTYSLVS
LSLVALLLTF SFLTCLKGLK SNTRGIHSNI SVTLFFSELL FLLGINRTEN QFLCTVIAIL
LHCFFLSTFA WLFVQGLHIY RMQTEARNVN FGAMRFYYAI GWGVPAIITG LAVGLDPEGY
GNPDFCWISV HDKLVWSFAG PITVVIVVKP CQKETKKKSV LVPTCCEGLS LQPSCSRLLS
PQGLAVLVLF CVLNEEVQEA WKLACLGKKG QSEEAARSTQ GPSTYNNTAL FEESGLIRIT
LGASTISSVS SVRSARTHSS QRGYLRDNVT ARQGSALDHS LLGHAGPTDI DVAMFHRDAG
GDQDSDSDSD LSLDEERSLS IPSSESEENV RLRGRFPRQF KRAAHSERLL TNPTNTAPKG
KFCGLWQGSA VPRGGVGERL RLAMASLPLT EEFSPSPPAV CPSPDVDGND LMSYWPALGE
CEVHPCSLQK WGSERKLGFD INKDAANNNQ PDLALTSGDE NSLTQTQRQR KGILKNRLQY
PPALQGLPAV GRMTNELSWY KTSTLGHRAV PAASYGRIYS GAGSLSQPAS RYSSREQLDM
LMRRQMSREQ LSRNNSGECL ETVPSRHGSR EELDTIPSRH GAAQPGAMAA EMVLSRRPGQ
PRSEVLSEAD LEELGQRKPP SKTSTRDYLR KARCSASTAK SLLFRFIPVL RWLPRYPVKD
WLLGDIASGF SVGIMHLPQG LAYALLAGLP PVTGLYSSFY PVFLYFFFGT SRHNSVGPFA
VISVMIGSLT DSLVPSDDFL EFVNGTNDTV VNEAQRDAAR VELVATITVL TGIFQVALGL
LQFGFVVTYL SDPLVRGYTT ASSVHVLISQ LKNVFGVSVG EHSGPLSLFV VSEGLIDSLE
SPDVTFIEIC KKLPETNVGT LVTAIIAMVA IFIVKELNHK FSAKLPMPIP IELITIIIST
GISYGVNLNS KFGISVVGNI PSGMKPPVVP NTSYFGQVVG NAFAIAVVGY AICISLGKIF
ALKHGYKVDS NQELIALGLS NFLGGFFQCF AISCSMSRSL VQESTGGNSQ VAGVISSLVI
LVTILKIGEL FRDLPKAILS AIIIVNLKGM FKQFSDLRML WKSNRVDLMI WVVTFIATLL
LNLDIGLAVS VAFALLTVIF RTQLPHYSIL GRVTDTDVYK DVAEYEKAQE VPGIKIFRSS
STIYFANVEM YSDALKKKSG IDVDRLIEKK KKALKKLKKQ QKKAQKEKAK RKKDTDAECN
GPGVAVIELS GEEDGTPPEP TLRSLGLPQP NFHAVILDFS PVNFVDTVSI KILKNIFKDF
HEIEVDVFVA SCSASVFAQL ERGNFFSSTI TKHCFFPSVN DAVLHLNDRT RPAPAALLPL
TRNRGAATYA QTLQNIPETN VTTLDNGLRV ASEESSQPTC TVGVWIGAGS RYENEKNNGA
GYFVEHLAFK
//
