ID A0A452GKD4_9SAUR Unreviewed; 2029 AA.
AC A0A452GKD4;
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:ENSGAGP00000002069.1, 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:ENSGAGP00000002069.1}
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; ENSGAGT00000002356.1; ENSGAGP00000002069.1; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2029
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019298613"
FT DOMAIN 68..103
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 72..82
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 93..102
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2029 AA; 227900 MW; 6E1485129863782D CRC64;
LTLLCSAVIC AADCGGHGIC VGGTCRCEEG WMGAACDQRA CHPRCNEHGT CRDGKCECSP
GWNGEHCTIE GCPGLCNGNG RCTLDMNGWH CVCQLGWRGA GCDTSMETAC GDGKDNDGDG
LVDCMDPDCC LQPLCHVNPL CLGSPDPLDI IQETQTPTSQ QNLHSFYDRI KFLIGKDSTH
VIPGENPFDG GHACVIRGQV ITSDGTPLVG VNISFVNNPL FGYTISRQDG SFDLVTNGGI
SIILHFERAP FITQEHTLWL PWDRFFVMET IVMRHEENEI PSCDLSNFAR PNPVVSPSPL
TAFASSCSEK GPIVPEIQAL QEEINIAGSK IKLSYLSSRT AGYKSVLRIS MTHPTIPFNL
MKVHLMVAVE GRLFRKWFAA APDLSYYFIW DKTDVYSQKV YGLSEAFVSV GYEYESCPDL
ILWEKRTAVL QGYEIDASKL GGWSLDQHHA LNIQSGILHK GNGENQFVSQ QPPVIGSIMG
NGRRRSISCP SCNGLADGNK LLAPVALTCG SDGSLYVGDF NYIRRIFPSG NVTNILELRY
TRHHSPAHKY YLTSDPITGS IYLSDTNSRR IYKIKSTSVV KDVVKNSEVV AGTGDQCLPF
DETRCGDGGK GTEATLTNPR GKTQSLLTSI LKWASRKVPN QQFWNTTEQV YKLPQGNPLM
CLRVRLEWPT DLAVSPMDNS LYVLDNNVVL QISENHQVRI VAGRPMHCQV PGIDHFLLSK
VAIHATLESA TALAVSHNGV LYIAETDEKK INRIRQVTTN GEISLVAGAP SSCDCKNDAN
CDCFSGDDGY AKDARLNAPS SLAVCADGEL YVADLGNIRI RFIRKNKPYL NTQNLYELSS
PIDQELYLFD TSGKHLYTQS LPTGDYLYNF TYTGDGDITL ITDNNGNLVN VRRDSTGMPL
WLVVPDGQVY WVTIGTNSAL KSVTAQGHEV GMMTYHGNSG LLATKTNENG WTTFYEYDSF
GRLTNVTFPT GQVSSFRSDT DRSVHVQVET SSKDDVTITT NLSASGAFYT LLQDQVRNSY
YIGADGSLRL MLANGMEVAL QTEPHLLAGT VNPTVGKRNV TLPIDNGLNL VEWRQRKEQA
RGQVTVFGRR LRVHNRNLLS LDFDRVTRTE KIYDDHRKFT LRILYDQAGR PSLWSPSSRL
NGVNVTYSPG GHIAGIQRGT MSERMEYDQA GRIISRIFAD GKSWSYTYLE KSMVLLLHSQ
RQYIFEFDKN DRLSSVTMPN VARQTLETIR SIGYYRNIYR PPEGNASVIQ DFTEEGQLLH
TFYLGTGRRV IYKYGKLSKL AEMLYDTTKI GFTYDETAGM LKTINLQNEG FTCTIRYRQI
GPLIDRQIFR FTEEGMVNAR FDYNYDNSFR VTSMQAVINE TPLPIDLYRY DDVSGKTEQF
GKFGVIYYDI NQIITTAVMT HTKHFDAYGR MKEVQYEIFR SLMYWMTVQY DNMGRVVKKE
LKVGPYANTT RYSYEYDADG QLQTVSINDK PLWRYSYDLN GNLHLLSPGN SARLTPLRYD
LRDRITRLGD VQYKMDEDGF LRQRGNDIFE YNSAGLLIKA YNKVSGWSVK YRYDGLGRRV
SSKTAHSHHL QFFYADLTNP TKVTHLYNHS SSEITSLYYD LQGHLFAMEL SSGDEFYIAC
DNIGTPLAVF SGTGLMIKQI LYTAYGEIYM DTNPNFQVII GYHGGLYDPL TKLIHMGRRD
YDVLAGRWTS PDHDMWKHLS SNNIMPFNLY MFKNNNPISN AQDIKCYMTD VNSWLLTFGF
QLHNVIPGYP KPDTDAMEPS YELIHTQMKT QEWDNSKSIL GVQCEVQKQL KAFVTLERFE
QIYSSSIAGC RTVKENKNFA SGGSVFGKGV KFAMKDGRVA TDIISLANED GRRIAAILNN
AHYLENLHFT IEGVDTHYFV KQGPSESDLS ILGLSGGRRT LENGVNVTVS QINTVLSGRT
RRYTDIQLQY GALCLNTRYG TTLDEEKARV LELARQRAIA QAWAREQQRL RDGEEGIRSW
TEGEKQQVLN TGRVQGYDGY FVISVEQYPE LSDSANNIHF MRQSEMGRR
//
