ID A0A452H8B3_9SAUR Unreviewed; 766 AA.
AC A0A452H8B3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000011007.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000011007.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000011007.1}
RP IDENTIFICATION.
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}.
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DR STRING; 38772.ENSGAGP00000011007; -.
DR Ensembl; ENSGAGT00000012604.1; ENSGAGP00000011007.1; ENSGAGG00000008524.1.
DR Proteomes; UP000291020; 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:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR CDD; cd15439; 7tmB2_EMR; 1.
DR CDD; cd00054; EGF_CA; 3.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
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; IPR001740; GPCR_2_EMR1-like_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR PANTHER; PTHR12011:SF449; ADHESION G PROTEIN-COUPLED RECEPTOR E1; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR01128; EMR1HORMONER.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
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};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 493..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..585
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..58
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 70..107
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 157..195
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 495..741
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
SQ SEQUENCE 766 AA; 82538 MW; 568CE2904FEFBCC7 CRC64;
MPGAGTCLLP SFPPIKGRLH YMDECLDLAS CPAHATCTNT PGSHYCTCNT GFASSSGEQR
FTDPAVQCND LDECSRDPSP CGPSSICTNT GGSYTCTCPP GYLPRSQAGI RFSCAALGVX
SEQLCLPSLG CDCLQSPGKW GELAVSSLLA PQCCSVDVDE CAQTPAICGP SASCMNTPGS
YTCQCSPGHH PSTDGPWVPG TTRCTGDHPS NLPRPLTAAL AHEKDKIRDA FCMLLASTFS
VLGDPNERKN STISLEKAAE GFASILDQTP SWSNLSTEQV SIMATVFLEN VENVVLDVLK
NPTGNGSQTI QMKQLDLQTK VIEDSCPRKD SVVSLEVKGE TMKISCRTIQ GTVAQEAANS
SGFSLGILAA RAGVAFASYV GMESILNGSF FHGQRATSDW PVRINSRVVS AFLTSQAKTD
FPDPINYTFQ TIMPSSSPDK LICVSWEATD RRGSWSRAGC RVVRSNASHT TCSCNRISNL
AVLMASGEIT AGFPLFLISH VGLALSLLCL FLAILTFLLC RSIRNVNTSI HLQLCLCLFL
ADLLFLTAVD SPSHQLACAI IAGLLHYLFL ACFAWMFLEA VVLFLTVRNL GVVNYFSTHS
PKMWHLSLFG YSFPALVVAV SATVMPEGYG RQENCWLSME KGFIWSFLGP VCVIIGINSV
LFALTLWMLQ RKLFSLNTEV STLKNTRLLT FKAIAQVFIL GCTWIFGLLQ VGPAATVMAY
LFTIVNSLQG AFIFLVHCLL NRQVPPRAVR PLIDSADPLP AESRAG
//
