ID A0A6I8NRT6_ORNAN Unreviewed; 1458 AA.
AC A0A6I8NRT6;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Phospholipase A2 receptor 1 {ECO:0000313|Ensembl:ENSOANP00000043959.1};
GN Name=PLA2R1 {ECO:0000313|Ensembl:ENSOANP00000043959.1};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000043959.1, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000043959.1}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000043959.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR Ensembl; ENSOANT00000073126.1; ENSOANP00000043959.1; ENSOANG00000006157.3.
DR GeneTree; ENSGT01050000244842; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000006157; Expressed in adult mammalian kidney and 3 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 8.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 8.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR22803:SF124; C-TYPE LECTIN DOMAIN FAMILY 19 MEMBER A-RELATED; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 8.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 2.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 1394..1417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 180..228
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 249..363
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 394..511
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 531..645
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 686..806
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 828..947
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 973..1098
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1129..1231
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1264..1385
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 185..211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 199..226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1458 AA; 167800 MW; 9A3E657A47490E55 CRC64;
MLLYTFLSNN STFLSIWTAS KKNIISCYSY VDIIVTQRFF FLSGKGIFMI QSDYLRTCIS
SGKNGLVLQD CHQPTKNMLW KWVSKRHLFN LGSSGCLGLN ISNEEQPLGL YECDSPHSSL
WWHCNRKVVV GASQYALEIK NYNLVVARRQ SSHEWVQYLS DGDDICEHPF QELYTIQGNS
QGRPCVFPFR YNNQWFYECT KEGRKDGLLW CATTSQYEKD QTWGFCPNPG RYEIGCKVFW
EKDPDTNICY QFNLNSFLSW NEARSSCKMQ GGDLLSITHW KEENFIQKFL SVKEVKKVWI
GLNQLDEVNG WQWSDGTPLI HLNWDPDVNF DPFVQYHCGT FNSLLWDSWQ NHDCESPLPY
VCKKHLNHTK RELLAEKNTW KYYPTHCEPS WHPYNGNCYR LQKEEKNWTA ALHSCQSIKS
KLINMASLAE VEFLVNLLKD ENVSETWIGL SSGRNPVFFD WSGGSSATFT LWHKQQPNTF
PNGSRLCVSA DKTGGHWKVR NCEETLFYIC KNAGKVLSEA KSGCQEGWER HGGFCYKIDL
IRRSFDQASR GYYCPPSLVT VTNRFEQAFI TNMISSVVKT EDSYFWIALQ DQNVTGEYTW
KVRGQEYQPV QYTNWNKYQP RYNGGCVVMR GGNPPGLWEV KDCQRFRAMS LCKQPLNPHP
ETQREKIWPF EPCFLGWESK PNLPSCYKVF HSEKVLMKRT WSEAEALCED FGAHLASFSH
IDEEDFVNEM VLSKFNRTEE RQFWIGFNKR NPLSGGSWEW SDGTPVISSF LDDMYIGEDA
RNCAIYQTNK TVLPLRCGSK REWICKLPKD VRPMIPKWYQ YDGPWLFHHG TEYLFHTSAT
EWANFELVCQ LLDSNLLTIH SAEEQEFVQN KIKTLSKSDV NWWMGLHKMG PNDGFCWKDG
SPLIFQNWDK GRERSGQNQR QRCGFISSET GLWGDDDCSV AMPSICKRKK IWITEKDLSE
QPHGLCPKGW LYFGSKCFLV EIPKDPSKLK SWKSAQDSCA EEDGVLASIE NEVEQAFITM
NLFGQKANVW IGLQNSDYEE WLNGKHVAYS NWLPVDIINS QSLNTTKLRE QVHLCALLSS
NPNFHFTGKW YLEDCGKESY GYICEKMQDT SKHNTNASTM YPTSSTLQYG NRTFKVIGGN
MTWYMALDIC AANGAELVSI TDQFRQSFLT VLVNQLGHAH WIGLFTSDNG LNFEWSDGTK
SSFAYWEDES PSLGGCTLVD INGGWKSADC ETLLQGAVCH VPTETSLSEF KGLCSETSFP
WVKLKNNCYS FSTVLQSMSF DAAQKFCKGQ GSNLLTIKEE VENSFLLEEL HAYHSSVPMV
WLNAQFDSNN GTITWFDGSP AELSNWGIRE PDLDRFKTQL CIAMNTKDAV WQLCPCTEKK
GFICKMETAP SHGFIPLAVT VTLIVILGFS TFSFCLYKLN SRLFRRFSAF RITYYTSTNS
GIAPLEENIL ISDLERYD
//
