ID L5LG88_MYODS Unreviewed; 1240 AA.
AC L5LG88;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 3 {ECO:0000313|EMBL:ELK25000.1};
GN ORFNames=MDA_GLEAN10023143 {ECO:0000313|EMBL:ELK25000.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK25000.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000256|ARBA:ARBA00010933}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KB112367; ELK25000.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LG88; -.
DR eggNOG; KOG0236; Eukaryota.
DR eggNOG; KOG4289; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 8.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 7.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24026:SF38; CADHERIN EGF LAG SEVEN-PASS G-TYPE RECEPTOR 3; 1.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR Pfam; PF00028; Cadherin; 6.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; Cadherin-like; 7.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 7.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Receptor {ECO:0000313|EMBL:ELK25000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 2..40
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 41..146
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 147..251
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 252..353
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 354..456
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 457..562
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 563..664
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 712..918
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 921..957
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 966..1004
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1044..1131
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DISULFID 947..956
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 994..1003
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1240 AA; 135417 MW; A907BC0D9EBABBC7 CRC64;
MESYELVVEA NDQGQEPGPR SATVRVHITV LDENDNAPQF SEKRYVAQVR EDVRPHTVVL
RVTATDRDKD ANGLVHYNII SGNSRGHFAI DSLTGEIQVV APLDFEAERE YALRIRAQDA
GRPPLSNNTG LASIQVVDIN DHAPIFVSTP FQVSVLENAP LGHSVIHIQA VDADHGENAR
LEYALTGVAP DTPFVINSAT GWVSVSGPLD RESVEHYFFG VEARDHGSPA LSSSASVTVT
VLDVNDNRPE FTTKEYHLRL NEDAAVGTSV VSVTAVDRDA NSAISYQITG GNTRNRFAIS
TQGGAGLVTL ALPLDYKQER YFKLVLTASD RALQDHCYVH INITDANTHR PVFQSAHYSV
SVNEDRPVGS TVVVISASDD DVGENARITY LLEDHLPQFR IDADSGAITL QAPLDYEDQV
TYTLAITARD NGIPQKADTT YVEVMVNDVN DNAPQFVASH YTGLVSEDAP PFTSVLQISA
TDRDAHANGR VQYTFQNGED GDGDFTIEPT SGIVRSVRRL DREARPVYEL TAYAVDRGVP
PLRTPVSIQV TVQDVNDNAP VFPAEEFEVR VKENSIVGSV VAQITAADPD EGPNAHVMYQ
IVEGNIPELF QMDIFSGELT ALIDLDYEAR QEYVIVVQAT SAPLVSRATV HVRLVDQNDN
SPVLNNFQIL FNNYVSNRSD TFPSGVIGRI PAYDPDVSDR LFYSFERGNE LQLLVVNQTS
GELRLSRQLD NNRPLVASML VTVTVQPSGL LFYNGRLNEK HDFLALEIVA GQVRLTYSTG
ESSTVVSPTV PGGLSDGQWH TVHLRYYNKP RTDALGAAQG PSKDKVAVLS VDDCDVAVAL
QFGAEIGNYS CAAAGTQTSS KKSLDLTGPL LLGGVPNLPE NFPVSHKDFV GCMRDLHIDG
RQVDMAAFVA NNGTVAGCQA KLHFCDSNPC QNHGRCAERW GGFSCDCPVG FGGRDCRLSY
YGPGCVDACF LNPCQNQGSC RHLPGAPHGY TCDCVDGYFG QHCEHRMDQQ CPRGWWGSPT
CGPCNCDVHK GFDPNCNKTD GRCHCKEFYY RPRGSDACLP CDCYPVGSTS RSLLYDACPK
SLRAGVWWPQ TKFGLLASVP CPRGALGAAV RLCDEDKGWL EPDLFNCTSP AFRELLLLLD
GLELNRTALD TVEAKKLAQR LREVTDHTDH YFSQDVRVAA RLLAHLLASE SHQQGFGLTA
TQDARFNEVG CALCSPRSLA LDSEPWVPTQ ALLTLGKGRS
//
