ID G1K3H7_XENTR Unreviewed; 2356 AA.
AC G1K3H7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Protein NDRG2 {ECO:0000313|Ensembl:ENSXETP00000035239};
GN Name=ndrg2 {ECO:0000313|Ensembl:ENSXETP00000035239};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000035239};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000035239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000035239};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000035239}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2011) to UniProtKB.
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. 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}.
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DR ESTHER; xentr-ndrg2; Ndr_family.
DR Ensembl; ENSXETT00000035239; ENSXETP00000035239; ENSXETG00000016160.
DR AGR; Xenbase:XB-GENE-951910; -.
DR Xenbase; XB-GENE-951910; ndrg2.
DR HOGENOM; CLU_035361_1_0_1; -.
DR InParanoid; G1K3H7; -.
DR TreeFam; TF313168; -.
DR Bgee; ENSXETG00000016160; Expressed in skeletal muscle tissue and 26 other cell types or tissues.
DR ExpressionAtlas; G1K3H7; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 9.
DR CDD; cd00054; EGF_CA; 5.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 1.25.40.610; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 9.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
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; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24026:SF32; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 2; 1.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; Cadherin-like; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 5.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_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; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; 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 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 Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 2131..2153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2165..2181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2187..2211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2232..2252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2272..2292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2324..2345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..142
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 143..248
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 249..354
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 355..457
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 458..560
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 561..663
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 664..770
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 771..872
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1135..1171
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1175..1213
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1214..1418
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1394..1430
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1565..1601
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1602..1639
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1696..1743
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1728..1801
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2128..2297
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 1968..1990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1971..1990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1161..1170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1420..1429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1591..1600
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1629..1638
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1696..1708
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1698..1715
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1717..1726
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2356 AA; 259269 MW; 1EF0E68D86EAD448 CRC64;
MLIWDIVLSQ SDIHTGSGLG AARYKRNVNL SPQFHSPTYQ VSVPENKPAG TFVVQLRASD
PDEGESGKLE YSMDALFDSR SASYFSLDSN TGVVTTSGEL DRETKSTHVF RVTVRDGGIP
SRTAMATLTV TVSDTNDHDP NFEQQEYRET VRENMEVGYE VMTVRATDGD SLGNANIAYR
LISGGREVFE IDPRSGVIRI LGPVDREEIA SYQLVVEAND QGHDPGPRSS TATVHITIQD
ENDNAPQFSE KRYVARVSED SSIESQLLVV TATDCDQGAN AAVHYSILSG NSRGLFSIDP
LTGAIFLAGT LDFETGREYT LRVRAQDGGR PPLSNVTGLV IIQVLDVNDN APNFVSGPFQ
ASVLENAPIG YSVLQVQALD ADSGDNARLD YCLSGTTGPF SINNSTGWIM IQTELDREEI
EFYNFIVEVW DRGQPSLSSS ASVSVQVLDV NDNAPEFTQS EYHARLNEDA AVGSSVLTVW
AADRDAYATI TYQITAGNTR HRFSISSLSD SQGLLTLALP LDYKLERQFV LTITASDGMR
SDTARAIVNV TDANTHRPVF QSSHYTVSVK EDQPAGTTVV VISATDEDTG ENARIAYLAE
EGLPQFAIDP ETGAVTTTME LDYEDQVSYT LAVTAHDHGI PQKSDTTYLE ILVIDVNDNP
PVFQRASYKG SVPEDSPPYT SVLQVSATDR DSGLNGRIFY TFAGGDDGDG DFTVEYTSGI
VRTLRQLDRE NVVEYRLTVY AVDKGHPLPH RTPAEVLVTV LDVNDNAPVF AREELEVKVF
ENSPLGPPLA RITATDPDEG PNAQIMYQIV EGNIPEVFQL DIFSGELTAL VELDYEERSE
YTIVVQATSA PLVSRAIVRV CLVDVNDNAP TLSDFRVVFN HYVGGGGSFP DGVIGRVPAR
DPDVSDVLTF NFLHGNELAL LRLNTSSGEL QLSHDLDNNR PFEATMNIEV TDGKHRVTAQ
CTLQVSIITD ELLSHSITLR LGGISQHQFL SPLLPLFTQA VAQVLSISPQ SVVVFSIKDD
AEEPTTVQSD RQILNVSLLV QGAEEFLPSE KLRELLYLNR TLLGALAQQR VLPFDDNVCL
REPCPNYMLC VSALRFDSSA PFLASDTLLF RPILPVGGLR CRCPIGFAGD YCETEIDLCY
TRPCGEHGIC QSHEGGYTCQ CEEAYTGTHC EISLRSARCS TGLCKNGGMC VNLLVGGFYC
ECPPGGYDAP YCAVSTRSFH GGSFLTFRGL RQRFHFTISL SFATRERNGL LLYNGRFNGK
HDFIVLEITN EQIQLTFSAG EFTTVVSPFV PGGVSDGQWH TVHLHYFNKP VVGQSGELLG
PSDQKVAVVA IDDCDTEMSL QFGDMLGNYS CAAKGMQSGT KKLVTRNKGD LLRSGLLQDF
NQVACFSSES CLAKKNQCDG NSCQNGGTCV NRWDGYSCEC SLGYGGKNCE QEMLFPLRFL
GNGILSWEGL VLPLSIPWNL SLMFRTRQTD ALLLKAHDKR NCTVTLQVMD ASSVCFGLND
GIWHHITVEA KNDPAMPGTQ LVILDADYGQ EQVYYSFFYL GVRVGGSLLS LLNAESLNAE
KGCSFPDPCD SSPCPKHSYC RDDWDSYSCA CRHGFYGDNC TDACELNPCQ HQSTCVKRTS
YPHGYMCDCA SGYYGTYCEN RLDQPCARGW WGHPVCGPCN CDVNSGFDTD CNKTTGECRC
KDNHYRPVGA SFCLLCDCYA IGSISRTCHP VTGQCPCKPG VIGQHCDLCD NPFAEVTMSG
CEVNYDSCPR AVESEIWWPR TRFGLPAAVS CPRGSVGTAV RHCDEHRGWL PADLSNCTSS
AFITLKGLVR NIAMQAVKTL LDSDVRISYH LLSAILQQQS QESGFSLAAT QDVHFTENVV
KAGSMLLNLG TKKQWDNIQV SEAGTALLLR NFETYASTVA QNMKQTYLSP FIINTPNIGE
FVSVTQLDKL NFAGTVLPRY ETLRGIKPSD QETTVILPRA NFLPHTTYAP FASKDHEDKN
NSRKKRDRQH WEKVIPGDNQ AVVTVIIYHS LGLLIPQRFD PDKRSLRVPK RPVINSPVVS
INIHEAEGGA FDQPITVQFR LLDTQDRSKP ICVHWNHSIQ LPGGGWSARG CELVFRNETH
ISCQCHHMTS FAVLMDMSHR ENGEVLPLRA ITYPCLGLTL GFLLLSLLFL FILSSLHCNK
HSIHRNLILA LLLSQLSFML GVNQADMQFA CTFIAILLHF LSLCCFSWVF LEVLHLYRRL
TEVRDVNSGP MRFYYALGWG VPAFITGLAV GLDPEGYGNP DFCWLSVSDT LIWSFAGPVA
FVVSVKVLKL FVNVTVIKSS MCLVAYIPCC LALTPKTMSR TLKYLSGCVH SVSVWLLTCL
AHLALTPETV SRGLIY
//
