ID A0A674DTT5_SALTR Unreviewed; 1464 AA.
AC A0A674DTT5;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:ENSSTUP00000099432.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000099432.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000099432.1}
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 Ensembl; ENSSTUT00000106714.1; ENSSTUP00000099432.1; ENSSTUG00000044514.1.
DR GeneTree; ENSGT01050000244842; -.
DR Proteomes; UP000472277; Unplaced.
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; 7.
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; 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; 7.
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; SSF57440; Kringle-like; 1.
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; 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, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000472277};
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 1398..1421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..218
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 232..345
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 374..491
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 515..632
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 672..794
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 817..936
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 962..1088
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1117..1222
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1254..1377
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 175..201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 189..216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 1464 AA; 165831 MW; F72F713923BB23A3 CRC64;
MDKQYFFSFF KQRSFKRVCE HTFGPAEPKH MEALRQVLLG MFILESTQLK RCISSNLVLE
SCERPTRHML WKWVSRHRLF NLGSSLCLGL NISDSTQPLD TFECDSPLRT LWWRCNGNTL
YGASQLKLSV AGRLVVVKRS SYHQWRRYST PGEGPCAYPY EEIHTLLGNA HGMPCALPFK
YNNKWYSECT AEGREDHHRW CATTSRYDQD EKWGFCPSQE LGCDTFWDSN QESRACYQFN
LYTILTWSQA YSSCLAQGGS LLSITDLTEQ MYIRERLADV GVMVWIGLNH LSERTGWQWS
DGAPLALVNF TSGKRVGQCG VYNSASGGHQ WQSLSCESAL PYICKKTPND TRRAEPLDNW
LHYRTVCSEG WLAHNRYCYK ALAEAEAGSW EDSSAACNSV GANLTSLHSL SEVELLLGLL
ANGSGSEVWI GLIKKLSSSA VEWSDGSPVD LTLWHGHHPK HSNSQLCAKT DVKEGNWLLA
PCDEKLPAVC RRAGLLPLHP TGTWDEGCPE DWMRKGHSCY MVTSHEQSYE DAVKGYYCKA
PLVTVENRFE QAFLNSLVNE MGTNGRVYYW TALQDQGNHG EYSWLGGHNG STLPLLYTNW
NRHQPVSAGG CVAMTGGQAL GHWEVKDCKS QKALSVCKQS ISGYQEVLFP TVHIDAYAPC
PPGWESHSGL LHCYKAFHSE KVLMKRSWED ADFFCQALGA QLASFHHYKE QVFVKGLLHS
MFDGTEGRWF WVGLNKRDPQ SAGAWEWSDG TPAVSSFIED KNEEDDRHSC AVYSDLTNTL
LPQPCDTKHE WICKVPRGME LNKPYWYNDQ NEPWVFYRGA EYLLAKQPFP WEDVNLACMM
MGAHLLSVHS KEELRFIRER MGKCVFVCVF VCVCLCVCVC VCVCSWSDES AVDYQNWAEG
SSHDAPVKQK QCVTMSSISG QWSVGECGSL HAHVCKRRTV SVVETPREPH YLGGCPERWL
YFGHKCFLLH LPNSSEEGKS WRDSQSICSS FQGTLVAIED EIEQAYITML LQGRTVGVWI
GLRDEDTMKW TNGKPVSYTN WSPVEPKNPL TDEWLSGPLG GDDPLCTVLS NSHNFHLTGK
WFDEKCTESG YGFVCQKPQA KPPSHSYLHP LPDNIEYKNR RYRVVRGNMS WYEALHMCLE
SESELVSVTD PFHQAFLTVL VNRLAFPHWI GLYSQDDGIN YQWSDGSDTV FTHWDAVDDE
DFILGDCVYM DVTGGWRRAD CETPLQGALC HVPPPKSNAF TSYEVVCPLT WLRFGASCYN
FEPVVQRLTL EEAREHCKHK ANTSEVLTIQ TETENRFVLE QLWSYGFPHQ TVWLGMFFNT
DAGSMAWFDG SPMDYSNWNV KAPDPSLLAA DTCVSTRVSD GMWLLSQCTD RLGFVCKTNL
DTIPEVEVEP LNGLHHSVVP AAVLVAMLIF AVLVAVLWLV YKRNMTRFRR LPSLGNAYYR
HTSSQATDSD GNVLIADLEA HSGE
//
