ID A0A3B4CFZ7_PYGNA Unreviewed; 551 AA.
AC A0A3B4CFZ7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Complement component C1q receptor-like {ECO:0000313|Ensembl:ENSPNAP00000010388.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000010388.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000010388.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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_017567350.1; XM_017711861.1.
DR AlphaFoldDB; A0A3B4CFZ7; -.
DR STRING; 42514.ENSPNAP00000010388; -.
DR Ensembl; ENSPNAT00000017058.1; ENSPNAP00000010388.1; ENSPNAG00000015926.1.
DR GeneID; 108435793; -.
DR GeneTree; ENSGT00940000167312; -.
DR OMA; YCWVSSG; -.
DR OrthoDB; 19806at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR PANTHER; PTHR14789:SF4; ENDOSIALIN; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF14670; FXa_inhibition; 1.
DR PIRSF; PIRSF001775; CD93/CD141; 3.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 4.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..551
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017288342"
FT TRANSMEM 492..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..164
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 323..358
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 362..398
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 327..337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 551 AA; 59734 MW; 04DE3CDD31033684 CRC64;
MRALLLALSA LVAAWQAAGQ AAIWCTERAC YTLHDKRTPF EAAYTVCYKN GGYLLTMKDE
KEAEDVRIVL ELANDAGLFT SGEERLWIGL KLNRSNCVLN GEPLRGFHWV PDTADSGTFT
NWGRQPHSTC TEERCVSLQA AAAGSERLRW IDGSCKVGAL YACRFQFKGM CKPLTLAGPG
EVTYTVHFSN VPLNQSVNRL PHSTHADISC ASSGEKHYSF CTDAAAGGGF AWYPAKPFCE
SGERSCAFQN GGCSHVCSED RAGDVRCACK EGYHLGKDEF TCIPKNACQN APCEHECVVE
EASFACKCRK GYRLAQNWFG CVDEDECEQG VCGGHTCRNK PGSYECECKK GFRKDDTGAC
HDIDECAESA CREPAGCLNS QGSFSCYCSA GFRQAESGEC VDVDECVSRP CEDICTNTEG
SYKCSCRENF RLSENGISCV QVIVASPHTT ASNDALDRST AAITVTPLFS SEDSSTASAG
TERMESSARS PVLVWVLGSV IPLLLLVALT TVVAVLRCNR ARKAAKKKSA TADSYCWVSS
GFQAQPDTQP R
//