ID A0A337S858_FELCA Unreviewed; 750 AA.
AC A0A337S858;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Adhesion G protein-coupled receptor E2 {ECO:0008006|Google:ProtNLM};
GN Name=LOC101083497 {ECO:0000313|Ensembl:ENSFCAP00000042050.2};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000042050.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000042050.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000042050.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000042050.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000042050.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000042050.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000042050.2};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AANG04004050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A337S858; -.
DR Ensembl; ENSFCAT00000055859.2; ENSFCAP00000042050.2; ENSFCAG00000005648.6.
DR GeneTree; ENSGT00940000164113; -.
DR Proteomes; UP000011712; Chromosome A2.
DR Bgee; ENSFCAG00000005648; Expressed in tip of external ear and 2 other cell types or tissues.
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:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR003056; GPCR_2_ADGRE2_ADGRE5.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR PANTHER; PTHR12011:SF328; ADHESION G PROTEIN-COUPLED RECEPTOR E2; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR01278; CD97PROTEIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..750
FT /note="Adhesion G protein-coupled receptor E2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023894913"
FT TRANSMEM 453..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 513..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 602..628
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 676..699
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..101
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 454..700
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
SQ SEQUENCE 750 AA; 81852 MW; EBA286F1D5455987 CRC64;
SGGRDVPLLT VVLVPTASAP TDCAQWCPPK SSCVNATACR CSPGFTSSSG DVFTNRLENC
DDINECGPPP RVSCGKFAHC LNTEGSYHCT CGPGYELASG AKTFRSESEN TCQGKNHPTP
SISRWEGICS TFSRHQRAVL GTYPVTHPSL NPKAQNLLQR VTSESSEPLP PNTYKDRCNF
FPSWTPPRGI KSQRLSRFFE KVEDLARKFI PAFAQDSIQG LIEGVDELLQ TPEDLGALPR
SEQHRVAANL LAGLEDVLRN ISQALPNGTL TFNASAGTDL SLKVQEQGDR NVTLSLNQAK
MLLSLDEVHE SSDSGPSVVG LVSTPGMAKF LAEAPLVLDP KQQAVLREHK ELLGEVPPVL
LSGVVSAFVS NKDTQNLGSP VTFIFSHHSV TPGPTQKVFC VFWEHSQDGG GHWSTTGCRM
AATGDASTTC QCSHLSSFAV LMAHGHVQEE DPVLAVITYV GLGLSLLCLL LAALTFLLCK
AIQNTSTSLH LQLSICLFLA HLLFLTAIDQ TKIKLLCAII AGALHYLYLA SFTWMLLEGL
HLFLTARNLM VVNYSSMSRF TKRLMFPVGY GVPALIVAVS AASRPSLYGT PTRCWLHTEK
GFVWTFLGPV CTIFSINLAF FLMTFWIVRN KLSSLNRDVS TLQNTRMLTF KATAQLLILG
CTWCLGLLQV GPAARVIAYL LTIINSLQGM FIFLVYCLLS QQVREQYGKW FRGVRKAKAE
PENYTLSSRT VSDASKHSAV RLCSVPRALP
//
