ID A0A3Q4I6W0_NEOBR Unreviewed; 1031 AA.
AC A0A3Q4I6W0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Secretory phospholipase A2 receptor-like {ECO:0000313|Ensembl:ENSNBRP00000026057.1};
GN Name=PLA2R1 {ECO:0000313|Ensembl:ENSNBRP00000026057.1};
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:ENSNBRP00000026057.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000026057.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q4I6W0; -.
DR Ensembl; ENSNBRT00000026748.1; ENSNBRP00000026057.1; 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; 5.
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; 7.
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: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; 5.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00034; CLECT; 5.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 7.
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; 5.
DR PROSITE; PS00023; FN2_1; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 965..988
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..182
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 199..303
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 384..496
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 540..661
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 766..871
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 901..956
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 139..165
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 153..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1031 AA; 117871 MW; 9DC77838703EF1B8 CRC64;
KGLFILESEP LKQCISANRS KLVLEDCERP TRRMLWKWVS QHRLFNLGTS ACLGLNISDS
TQPLGMFECD VSLPVLWWRC NGNTLYGASQ WRVTVIRGLV AVKKNIYHQW KRYNTPREGP
CSYPYEIHTL LGNAHGMPCA FPFKYNNQWY SECTTEGRED HLLWCSTTPR YDKGERWGFC
PVQSGCEHFW ESNQELRACY QFNLYTIQTW SQALSTCQAQ GGNLLSITSL AEHKYIRMVW
TGLNHIKDGH GWQWSDGAPL SLVNFTTLPA SPLQDNKQCG VYSGFEGHWQ SLSCESALPY
ICKKTPNGTR GAEPLNWQYI DTECADGWWP HNGFCYRVLP EAEVGSWAES SQECHSYGAN
LTSIHSLSEV EMLVNLLANG WKKHGHSCYM VTGQEQSYED ALMGYYCKGS LLTVENFEQA
FVNSLLSESG AKSSMYYWIG LRDQDKGRKG EYRWLHHNGS SLPLTFTNWN KHQPSTGGCV
AMSGGPALGR WEVKDCKVHK ALAVCKQNIR SYHDVQLPEH HIDAYAPCPP GWESNSGLLH
CFKVFHSEKV LMKRSWVEAD FFCQALGAQL ASFQHYEEQV FVKQLLGTMF ETEARRFWVG
LNKRDPEYAG AWEWSDGSPV VTSFIDDKNE EDDRRDCAAY SDLTNTFMPQ LCDSKHEWVC
KLSRDKLNKP YWYTESEPWV FYRGAEYLLA KQPFDWHAVS LACQMMGAYL LSIHSKEELN
FVKEKWALSR CSDLHGYVCK RETVSVVETP REPHYIGGCP EKWLYFGHKC LLLHLPTSPK
EGKSWNDAQS ICSSFQGSLV AIEDEIEQFI TMFLQGSAVG VWIGLRDEDT MKWTNGRPVS
YTNWDEPLCT VLSNNHNFHL TGKWYDEKCS ESGYGFVCQK PQPSKRPTHS YHHLLPEIIE
YRNRNYKVVT GNLSWYDAMN KCKGHDSDLV SVTDAYHQAF LTFLVNRLGA PHWIGLYSVD
LHHGVIPAAV LAALLIFILL AGVMWFLYKR SSGRFQRLPT LGSAYFRQTD SQATESDGNV
LIADLEPPSA E
//
