ID G3NXW3_GASAC Unreviewed; 614 AA.
AC G3NXW3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Zmp:0000001114 {ECO:0000313|Ensembl:ENSGACP00000010183.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000010183.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000010183.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000010183.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR AlphaFoldDB; G3NXW3; -.
DR STRING; 69293.ENSGACP00000010183; -.
DR MEROPS; S01.302; -.
DR Ensembl; ENSGACT00000010205.1; ENSGACP00000010183.1; ENSGACG00000007677.1.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000155418; -.
DR InParanoid; G3NXW3; -.
DR OMA; KLWVCDH; -.
DR TreeFam; TF330647; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000007677; Expressed in zone of skin and 5 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006956; P:complement activation; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR024175; Pept_S1A_C1r/C1S/mannan-bd.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001155; C1r_C1s_MASP; 2.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR001155-4};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR001155-2};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001155-4};
KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR001155-3};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Serine protease {ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 11..127
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 135..248
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 375..611
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 416
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 468
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT ACT_SITE 562
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-1"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-4"
FT MOD_RES 147
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-3"
FT DISULFID 64..87
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 198..211
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 260..278
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 272..287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 289..340
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 289..301
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 296..314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 308..323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 328..354
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 328..340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 348..363
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 365..488
FT /note="Interchain (between heavy and light chains)"
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 533..547
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
FT DISULFID 558..587
FT /evidence="ECO:0000256|PIRSR:PIRSR001155-2"
SQ SEQUENCE 614 AA; 67715 MW; 871046CF8A74048A CRC64;
MARNPRDTGE CFYRLEATAK TNTFLSPGYP EGYPPWSRCQ WQIRASEDQA VFVSFPFFDI
EDDCANDFVA IFDSLSPDDS QAITAKCGKR PPSNPLAVLS SGNIMLINFI TKANHQRSGF
EATYSAIPMS QVQTCGGVLS GVEGTFSSPL YPSFYPPAVD CKWTIKTAVA VLSVAGKEVR
LKFTMFRMKE PRVDISVCHK DYVEVMGTKY CGELSSLVLT STNSILDVIF HSDESFTDKG
FSCIYSAYDP ANPCPNKFAC ASGLCIKKEL HCDGWNDCGD LSDETKCNCD ADQYSCANGL
CKPKLWVCDR VDDCGDGSDE KSCTQGVCSD FNFKCKNAEC VNKLNAECDR VKDCSDNSDE
DNCGCGTRPY KLNRIVGGQN AELGEWPWQV SLHFKTMGHV CGASIISDKW LLSASHCFIT
SDNDHLVPSN WQTYSGMQDQ YKLDDIQLRL VQRIITHPDY NQMTFDYDVS LLELSKPLEF
TNTIQPICLP SPSHVFPPGM TCWVTGWGAL REGGSKSQRL QKAMVKIIND TVCNTVTEGQ
VTSRMLCSGF LSGGVDACQG DSGGPLACFE ESGKWFQAGI VSWGEGCARR NKPGVYSRVT
KLIEWINLGV PSLV
//
