ID A0A452GKC8_9SAUR Unreviewed; 2100 AA.
AC A0A452GKC8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
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:ENSGAGP00000002064.1, 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:ENSGAGP00000002064.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC {ECO:0000256|ARBA:ARBA00009385}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR Ensembl; ENSGAGT00000002350.1; ENSGAGP00000002064.1; ENSGAGG00000000665.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.180.10.10; RHS repeat-associated core; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR022385; Rhs_assc_core.
DR InterPro; IPR031325; RHS_repeat.
DR InterPro; IPR028916; Tox-GHH_dom.
DR InterPro; IPR006530; YD.
DR NCBIfam; TIGR03696; Rhs_assc_core; 1.
DR NCBIfam; TIGR01643; YD_repeat_2x; 2.
DR PANTHER; PTHR11219; TENEURIN AND N-ACETYLGLUCOSAMINE-1-PHOSPHODIESTER ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR11219:SF9; TENEURIN-4; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF05593; RHS_repeat; 1.
DR Pfam; PF15636; Tox-GHH; 1.
DR SMART; SM00181; EGF; 3.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 136..171
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 140..150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 161..170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2100 AA; 235237 MW; 61D38B8FF3B59E52 CRC64;
PIEVWSQCSG GGAVHGAPCR PPSNHHHHHL GAGPAGHFPG AAQCQERLLT ARSAVLTGAA
RVPFQPGVLV ENQAPEICAA DCGGHGICVG GTCRCEEGWM GAACDQRACH PRCNEHGTCR
DGKCECSPGW NGEHCTIEGC PGLCNGNGRC TLDMNGWHCV CQLGWRGAGC DTSMETACGD
GKDNDGDGLV DCMDPDCCLQ PLCHVNPLCL GSPDPLDIIQ ETQTPTSQQN LHSFYDRIKF
LIGKDSTHVI PGENPFDGGH ACVIRGQVIT SDGTPLVGVN ISFVNNPLFG YTISRQDGSF
DLVTNGGISI ILHFERAPFI TQEHTLWLPW DRFFVMETIV MRHEENEIPS CDLSNFARPN
PVVSPSPLTA FASSCSEKGP IVPEIQALQE EINIAGSKIK LSYLSSRTAG YKSVLRISMT
HPTIPFNLMK VHLMVAVEGR LFRKWFAAAP DLSYYFIWDK TDVYSQKVYG LSEAFVSVGY
EYESCPDLIL WEKRTAVLQG YEIDASKLGG WSLDQHHALN IQSGILHKGN GENQFVSQQP
PVIGSIMGNG RRRSISCPSC NGLADGNKLL APVALTCGSD GSLYVGDFNY IRRIFPSGNV
TNILELRNKD FRHSHSPAHK YYLTSDPITG SIYLSDTNSR RIYKIKSTSV VKDVVKNSEV
VAGTGDQCLP FDETRCGDGG KGTEATLTNP RGKTQSLLTS ILKWASRKVP NQQFWNTTEQ
VYKLPQGNPL MCLRVRLEWP TDLAVSPMDN SLYVLDNNVV LQISENHQVR IVAGRPMHCQ
VPGIDHFLLS KVAIHATLES ATALAVSHNG VLYIAETDEK KINRIRQVTT NGEISLVAGA
PSSCDCKNDA NCDCFSGDDG YAKDARLNAP SSLAVCADGE LYVADLGNIR IRFIRKNKPY
LNTQNLYELS SPIDQELYLF DTSGKHLYTQ SLPTGDYLYN FTYTGDGDIT LITDNNGNLV
NVRRDSTGMP LWLVVPDGQV YWVTIGTNSA LKSVTAQGHE VGMMTYHGNS GLLATKTNEN
GWTTFYEYDS FGRLTNVTFP TGQVSSFRSD TDRSVHVQVE TSSKDDVTIT TNLSASGAFY
TLLQDQVRNS YYIGADGSLR LMLANGMEVA LQTEPHLLAG TVNPTVGKRN VTLPIDNGLN
LVEWRQRKEQ ARGQVTVFGR RLRVHNRNLL SLDFDRVTRT EKIYDDHRKF TLRILYDQAG
RPSLWSPSSR LNGVNVTYSP GGHIAGIQRG TMSERMEYDQ AGRIISRIFA DGKSWSYTYL
EKSMVLLLHS QRQYIFEFDK NDRLSSVTMP NVARQTLETI RSIGYYRNIY RPPEGNASVI
QDFTEEGQLL HTFYLGTGRR VIYKYGKLSK LAEMLYDTTK IGFTYDETAG MLKTINLQNE
GFTCTIRYRQ IGPLIDRQIF RFTEEGMVNA RFDYNYDNSF RVTSMQAVIN ETPLPIDLYR
YDDVSGKTEQ FGKFGVIYYD INQIITTAVM THTKHFDAYG RMKEVQYEIF RSLMYWMTVQ
YDNMGRVVKK ELKVGPYANT TRYSYEYDAD GQLQTVSIND KPLWRYSYDL NGNLHLLSPG
NSARLTPLRY DLRDRITRLG DVQYKMDEDG FLRQRGNDIF EYNSAGLLIK AYNKVSGWSV
KYRYDGLGRR VSSKTAHSHH LQFFYADLTN PTKVTHLYNH SSSEITSLYY DLQGHLFAME
LSSGDEFYIA CDNIGTPLAV FSGTGLMIKQ ILYTAYGEIY MDTNPNFQVI IGYHGGLYDP
LTKLIHMGRR DYDVLAGRWT SPDHDMWKHL SSNNIMPFNL YMFKNNNPIS NAQDIKCYMT
DVNSWLLTFG FQLHNVIPGY PKPDTDAMEP SYELIHTQMK TQEWDNSKSI LGVQCEVQKQ
LKAFVTLERF EQIYSSSIAG CRTVKENKNF ASGGSVFGKG VKFAMKDGRV ATDIISLANE
DGRRIAAILN NAHYLENLHF TIEGVDTHYF VKQGPSESDL SILGLSGGRR TLENGVNVTV
SQINTVLSGR TRRYTDIQLQ YGALCLNTRY GTTLDEEKAR VLELARQRAI AQAWAREQQR
LRDGEEGIRS WTEGEKQQVL NTGRVQGYDG YFVISVEQYP ELSDSANNIH FMRQSEMGRR
//
