ID K1RZC1_CRAGI Unreviewed; 1939 AA.
AC K1RZC1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Latrophilin-2 {ECO:0000313|EMBL:EKC40356.1};
GN ORFNames=CGI_10018684 {ECO:0000313|EMBL:EKC40356.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC40356.1};
RN [1] {ECO:0000313|EMBL:EKC40356.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC40356.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR EMBL; JH822105; EKC40356.1; -; Genomic_DNA.
DR HOGENOM; CLU_235033_0_0_1; -.
DR InParanoid; K1RZC1; -.
DR OMA; GAKKCTE; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0016525; P:negative regulation of angiogenesis; IEA:InterPro.
DR CDD; cd15040; 7tmB2_Adhesion; 1.
DR Gene3D; 2.60.220.50; -; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR008077; GPCR_2_brain_angio_inhib.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR12011:SF470; LATROPHILIN-LIKE PROTEIN LAT-2; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 2.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR01694; BAIPRECURSOR.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM01411; Ephrin_rec_like; 6.
DR SMART; SM00303; GPS; 2.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF111418; Hormone receptor domain; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 567..605
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 717..802
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 785..869
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 1164..1403
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DOMAIN 1506..1607
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DISULFID 595..604
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1576..1586
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1939 AA; 213435 MW; F89FC9C7BA849907 CRC64;
MASFWCAFSD RSCPRMYPCS NTFEHDILTD DGFRSPACRR SQFEPRCDKN IVEGWYVLHS
SDGSTTLRVH RECPRQTTCG TDNPIWMNGT YPAVADGIVE RQMCVRTGFG CCQDSFHVKV
KNCSNFLTFK LKPVPKCNQR YCFDRNECAP LTVTNTTPIN AEFTDDNLCP NGTYRKSNNN
ASQENRNNPC LSCPLGFVCA NGKKSPCPLG FYCPPGSSKA ELCRPGNYCP RGPHYPVQCK
AGFYNPANAS VNISACLPCP PGFYCFSKGL DSPTGPCLPG FYCSGSSTKA NPDDGIMGNL
CPPGHYCPRG SGQPIPCPEG FFNPTSIRSK CEICPKNLTC PEGSIYPFEC NSENVSLSVE
CSLRPAEPTI NPCSNPDGSR KYGICEDCPP GNLCKNGFNI SCPAGYFCPN GTSVFICPEG
FFCPAGRTSP MPCPIGTFNP YSGNGTEKAC LKCTPGLFCK DKGLSVPSGP CSPGFYCNGG
SVTPHPLNGH GGDICPVGHY CPEGTGLFTQ CPPSTYNPSR GQSNNRSCLA CPEGLTCNRS
GLALPSECYA NSTNITDALT DISCPEIGDY CSNNSKCLYD GTCRTNNKTW GFCECLPNYE
GSFCEIDKTL LFLMENSTLN YQTVEKEVVV MEIVFGTSFL QSDVNITWYR NDLMVRNSSR
VEITTDVADD YFRLYTTRLT IKSAREFYNG SAVVVASLPQ LGVSVSVNVS LTVVPLPVVT
VSPLSVSVQT GGAVVLTCSV QNLDPSNMAP TLEWVKDRDV LLSQQQNESM LTISNVQKDR
AGQYVCRLRY SVLGVNGTRK AAADVFVYSP DDLRCKKTVD EHGIHWEVGV TGMVYYALCP
ENYVGNASKL CKSDGTWERT VTINCVDKDI AEANQQLDDI LTNNIVDSSF VSSVVGKQMA
SLRNWTAQHI GTSTSGDVDR TVGLLDKVLQ ATDVANSKLP DNDFVNVVDN VLSEGQSKNW
RDINEQTKEG SSRILSTVEE FGQQVSKGLP SGEYKNYHAK NYFMTVGHGS TQESVTFPDS
PASDSTSLVL PVQSDPQGKE TVYSATIYRT AYTFLPIKNE LSGNGSRDTS YVNSDVLSMD
IIDEREKISL NPGIVLNIEH KTETDLEKTN VSCVFWNFTL RSWSSEGCNT TKVNGHVTRC
ECDHLTNFAI LMRPYREEEE DAILSLISLI GCSITVVLST ITFFIFMILW RYIKNDQNLV
LIHLCVSISL AYLLFLVGVT RTENKVVCTV IAAFLQYFFL VEFFLMLAMG VYYFLQITVL
YYSFSTANDI KARLNMKRLL PIAWVIPVFI TGITIGATYT REYNQSRVCW LSTESGSLYG
FVGPVLLIIC INLFIICSLF RVMCATRLLA ESNTKRKATT GLRSLCTLLP VLGITWVFGI
LSINEDLIAF QYLFAVREAL LKKMRLFESQ QENSKIQTKN SKRLSNVQEN LKKVKNDKEK
EANSTRRVTP PVRLIRYTKQ LDFIDGGHDN VCFDAMLPLD VVPLRRQSLS DSTPTTPGDS
VQDGAIRLVG GKNPFEGRVE IFHSGIWGTI CDDRWTYKEA GVICHMLGAM RENATVKANA
EYGNGVGSIW LDDVTCVGNE TSIVNCSHNE WGNHDCTHAE DVGVICVPTS DSQNSTGQWL
YNVDQALSIH TGTYTCGLDR CQRNLATVDV TDIPENECKA PLALNCERDK LDDVIAQIDF
LTKGDINSAD VDHAIKTALP KLADFVQEGI SNGESLDKTV DILHKMTSLA DASNVSIESA
IESSVDSILE AVSTFGNVIS KTVTLNSNIT LSRENLDFSY VATKFKSISE ILSGGSYSTN
GSHWSTDGCT VTRNHENITE CRCSHLTNFA ILVRPYQKET GSVEALKWIS IIGCCISVFF
CIITIVIFLV LWRCWLSLDS GALFGFLGPV ALIVLVSIVL LSNTVNLVIL ITLVITIYST
QLASTGTVRR KAVYVEMYR
//
