ID A0A3Q4N3Y6_NEOBR Unreviewed; 793 AA.
AC A0A3Q4N3Y6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Secretory phospholipase A2 receptor {ECO:0000256|ARBA:ARBA00044135};
DE AltName: Full=180 kDa secretory phospholipase A2 receptor {ECO:0000256|ARBA:ARBA00044310};
DE AltName: Full=M-type receptor {ECO:0000256|ARBA:ARBA00044268};
GN Name=PLA2R1 {ECO:0000313|Ensembl:ENSNBRP00000026329.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000026329.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000026329.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A3Q4N3Y6; -.
DR Ensembl; ENSNBRT00000027023.1; ENSNBRP00000026329.1; ENSNBRG00000019624.1.
DR GeneTree; ENSGT01050000244842; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000019624; Expressed in testis.
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; 4.
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; 4.
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; IPR013806; Kringle-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR PANTHER; PTHR22803:SF74; SECRETORY PHOSPHOLIPASE A2 RECEPTOR; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 4.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00034; CLECT; 4.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 4.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 4.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..793
FT /note="Secretory phospholipase A2 receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018789770"
FT DOMAIN 161..209
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 227..327
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 356..467
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 498..584
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 624..716
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 166..192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 180..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 793 AA; 90725 MW; 35F5BC96934327A3 CRC64;
RWPPLPEPGS AGGFFLLKGS LSFLLSPCLF ILESEPLKQC ISANRSKLVL EDCERPTRRM
LWKWVSQHRL FNLGTSACLG LNISDSTQPL GMFECDVSLP VLWWRCNGNT LYGASQWRVT
VIRGLVAVKK NIYHQWKRYN TPREGPCSYP YEDIHTLLGN AHGMPCAFPF KYNNQWYSEC
TTEGREDHLL WCSTTPRYDK GERWGFCPVQ VSGCEHFWES NQELRACYQF NLYTIQTWSQ
ALSTCQAQGG NLLSITSLAE HKYIRGTAHV KKDTRTEIKP TKPFYHLCPS DLPASPLQDN
KQCGVYSGFE GHWQSLSCES ALPYICKKTP NGTRGAEPLE NWQYIDTECA DGWWPHNGFC
YRVLPEAEVG SWAESSQECH SYGANLTSIH SLSEVEMLVN LLANCKDTEV WIGLWKQALL
PAVEWSDGSP VTLTLWVNHF IMFECIHHGT GNWLLASCDE RLAAVCRRES QNGVQHHGTW
DEGCPEVGKQ EYPQTHTSPN VFEQAFVNSL LSESGAKSSM YYWIGLRDQD KGRKGEYRWL
HHNGSSLPLT FTNWNKHQPG SPVTGGCVAM SGGPALGRWE VKDCKVHKAL AVCNYQHVSE
QRAHNGIHFC SLDPVFHSEK VLMKRSWVEA DFFCQALGAQ LASFQHYEEQ VFVKQTEARR
FWVGLNKRDP EYAGAWEWSD GSPNEEDDRR DCAAYSDLTN TFMPQLCDSK HEWVCKLSRG
KHAQTHSPAL STRTCCLYTH QDCIIYQTLF YIAGDKLNKP YWYTEPYLLS IHSKEELNFV
KERLRRVCYC RCS
//
