ID A0A383Z1A6_BALAS Unreviewed; 3292 AA.
AC A0A383Z1A6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 3 isoform X2 {ECO:0000313|RefSeq:XP_007168851.1};
GN Name=LOC103008968 {ECO:0000313|RefSeq:XP_007168851.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007168851.1};
RN [1] {ECO:0000313|RefSeq:XP_007168851.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007168851.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- FUNCTION: Receptor that may have an important role in cell/cell
CC signaling during nervous system formation.
CC {ECO:0000256|ARBA:ARBA00002066}.
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 -!- 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 RefSeq; XP_007168851.1; XM_007168789.1.
DR CTD; 1951; -.
DR OrthoDB; 4006628at2759; -.
DR Proteomes; UP000261681; Unplaced.
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:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 9.
DR CDD; cd00054; EGF_CA; 5.
DR CDD; cd00055; EGF_Lam; 2.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 9.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 7.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
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; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
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; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 9.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF111418; Hormone receptor domain; 1.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
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};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170,
KW ECO:0000313|RefSeq:XP_007168851.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..3292
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016641084"
FT TRANSMEM 2544..2568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2580..2600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2606..2628
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2649..2669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2689..2711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2732..2751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 324..431
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 432..543
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 544..649
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 650..754
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 755..856
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 857..959
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 960..1065
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1066..1167
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1373..1431
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1433..1469
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1473..1512
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1513..1717
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1720..1756
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1762..1942
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1944..1977
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1980..2018
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2075..2122
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2107..2185
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2545..2781
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 88..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2365..2407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2890..2920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2957..2986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3065..3116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3129..3221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3235..3292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2377..2395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2958..2979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3087..3102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3141..3156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3235..3282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1421..1430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1459..1468
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1746..1755
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2008..2017
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2075..2087
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2077..2094
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2096..2105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 3292 AA; 356002 MW; 0E60F6879855153E CRC64;
MARRRPWWGL RGPTTPLLLL LLLLSLFPPS REELGGGGGQ GWDPGVAAAT GPGARIGGGA
LALCPESPGV REDGKPGLGV REPVFVGLRG GKQSDQSGRG PPEQPGLGAE YGVKTFGSRG
QETGQGPGSL LCWRPEVSSC GRTGPLQRDS LLPERLSPEV PGPENSSPFP SDLRIRPCGS
QPVFSQRNTG RGAPQKVGTT RCCGELWAPG CRGQSERTKT SQARRAGPRP DRPPEAVGSG
PGQDSAPRKE RTASASGSAL RESRTAPEPT PERMRSRVLF RRRFLPQRPG PRPPGGPTEH
GAWRIPPASR VRPRRAANRH PQFPQYNYQA LVPENEAAGT AVLRVVAQDP DIGEAGRLVY
SLAALMNSRS LELFSIDPQS GLIRTEAALD RESMDRHYLR VTAQDHGSPR LSATTMVAVT
VADRNDHAPV FEQAQYRETL RENVEEGYPI LQLRATDGDA PPNANLRYRF VGPPAERAAA
SAAFEIDPRS GLISTSGRVD REHMESYELV VEASDQGQEP GPRSATVRVH ITVLDENDNA
PQFSEKRYVA QVREDVRPHT VVLRVSATDR DKDANGLVHY NIISGNSRGH FAIDSLTGEI
QVVAPLDFEA EREYALRIRA QDAGRPPLSN NTGLASIQVV DINDHTPIFV STPFQVSVLE
NAPLGHSVIH IQAVDADHGE NARLEYSLAG VASDTPFVIN SATGWVSVSG PLDRESVEHY
FFGVEARDHG SPPLSASASV TVTVLDVNDN RPEFTMKEYH LRLNEDATVG TSVVSVTAVD
RDANSAISYQ ITGGNTRNRF AISSQGGVGL VTLALPLDYK QERYFKLVLT ASDRALHDHC
YVHINITDAN THRPVFQSAH YSVSVNEDRP VGSTVVVISA SDDDVGENAR ITYLLEDNLP
QFRIDADSGA ITLQASLDYE DQMTYTLAIT ARDNGIPQKA DTTYVEVMVN DVNDNPPQFV
ASHYTGLVSE DAPPFTSVLQ ISATDRDAHA NGRVQYTFQN GEDGDGDFTI EPTSGIVRTV
RRLDREAVPV YELTAYAVDR GVPPLRTPVS IQVTVQDVND NAPVFPAEEF EVRVKENSIV
GSVVAQITAV DPDEGPNAHI MYQIVEGNIP ELFQMDIFSG ELTALIDLDY EARQEYVIVV
QATSAPLVSR ATVHVRLVDQ NDNSPVLNNF QILFNNYVSN RSDTFPSGII GRIPAYDPDV
SDHLFYSFER GNELQLLVVN QTSGELRLSR KLDNNRPLVA SMLVTVTDGL HSVTAQCVLR
VIIITEELLA NSLTVRLENM WQERFLSPLL GHFLEGVAAV LDTPAEDVFI FNIQNDTDVG
GTVLNVSFSA LAPRGAGAGS AGPWFSSEEL QEQLYVRRAA LAARSLLDVL PFDDNVCLRE
PCENYMKCVS VLRFDSSAPF LASASTLFRP IQPIAGLRCR CPPGFTGDFC ETELDLCYSN
PCRNGGACAR REGGYTCVCR PRFTGEDCEL DTEAGRCVPG VCRNGGTCAN GPDGGFRCQC
PVGGAFEGQR CEVAARSFPP SSFVMFRGLR QRFHLTLSLS FATVQPSGLL FYNGRLNEKH
DFLALELVAG QVRLTYSTGE SNTVVSPTVP GGLNDGQWHT VHLRYYNKPR TDALGGAQGP
SKDKVAVLSV DDCDMAVALQ FGAEIGNYSC AAAGTQTSSK KSLDLTGPLL LGGVPNLPEN
FPVSHKDFVG CMRDLHIDGR RVDMASFVAN NGTMAGCQAK LHFCDSGPCK NSGFCSERWG
GFSCDCPVGF GGKDCRLTMA HPHHFRGNGT LSWDFGNDMA VSVPWYLGLA FRTRAKQGVL
MQVQAGPHST LLCQLDRGLL SVTVTRGSGR AAHLLLDQVT VSDGRWHDLR LELQEEPGGR
RGHHVLMVSL DFSLFQDTLA VGSELQGLKV KRLHVGGLPP SSEEEAPKGL VGCIQGVWLG
STPSGSPALL PPSHRVNVEP GCVVTNACAS GPCPPHADCR DLWQTFSCTC WPGYYGPGCV
DACLLNPCQN QGSCRHLPGA PHGYTCDCVG GYFGHHCEHR MDQQCPRGWW GSPTCGPCNC
DVHKGFDPNC NKTNGQCHCK EFHYRPRGSD SCLPCDCYPV GSTSRSCAPH SGQCPCRPGA
LGRQCNSCDS PFAEVTASGC RVLYDACPKS LRSGVWWPQT KFGVLASVPC PRGALGLRGA
GAAVRLCDED QGWLEPDLFN CTSPAFRELN LLLDGLELNK TVLDTVEAKK LAQRLREVTG
HTDHYFSQDV RVTARLLAHL LAFESHQQGF GLTATQDAHF NENLLWAGSA LLAPETGDLW
AVLGQRAPGG SPGSAGLVQH LEEYAATLAR NMELTYLNPV GLVTPNIMLS IDRVEHPSPS
RGTRRYPRYH SNLFRGQDAW DPHTHVLLPS QAPRPSPPEV LSTSGSSMEN STTSSVAPPP
APPEPEPEPG ISIVILLVYR TLGGLLPAQF QAERRGTRLP QNPVMNSPVV SVAVFHGRNF
LRGVLESPIS LEFRLLQTAN RSKAICVQWD PPGPADQHGM WTARDCELVH RNGSHARCRC
SRTGTFGVLM DASPRERLEG DLELLAVFTH VVIAVSVAAL LLTAAVLLSL RSLKSNMRGI
HANVAAALGV AELLFLLGIH RTQNQLLCTA VAILLHYFFL STFAWLLVQG LHLYRMQVEP
RNVDRGAMRF YHALGWGVPA VLLGLAVGLD PKGYGNPDFC WISIHEPLIW SFAGPVVLVI
VMNGTMFLLA ARTSCSTGQR EAKKTSALTL RSSFLLLLLV SASWLFGLLA VNHSILAFHY
LHAGLCGLQG LAVLLLFCVL NTDARAAWTP ACLGRKAAPE EARPAPGTGP GAYNNTALFE
ESGLIRITLG ASTISSVSSA RSGRTQDQDS QRGRSYLRDN VLVRHGSAAD HTDHGLQAHA
GPTDLDVAMF HRDAGGGADS DSDSDLSLEE ERSLSIPSSE NVDGNDLLSY WPALGECEAA
PCALQTWGSE RRLGLDTSKD AANNNQPDLA LTSGDETSLG RAQRQRKGIL KNRLQYPLVP
QTRGTPELSW CRAATLGHRA VPAASYGRIY AGGGTGSLSQ PASRYSSREQ LDLLLRRQLS
RERLEEAPAP VLRPLSRPGS QERLDAVPGR LEPRDRGSTL PRRQPPRDYP GAVAGRFGSR
DALDLGAPCE WLSTLPPPHG ARDLDPQPPP LPLSPQRQLS RDPLLPSRPL DSLSRSSNSG
ERLDHVPSRH PSREGLGPPP QLLRVRGDPA SGPSHGPSTE QLDILSSILA SFNSSALSSA
VQSSSTPSGP HTTATLSATA SALGPSTPRS ATSHSISELS PDSEVPRSEG HS
//
