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Database: UniProt
Entry: A0A8B9PUR8_APTOW
LinkDB: A0A8B9PUR8_APTOW
Original site: A0A8B9PUR8_APTOW 
ID   A0A8B9PUR8_APTOW        Unreviewed;       469 AA.
AC   A0A8B9PUR8;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAOWP00000016946.1};
OS   Apteryx owenii (Little spotted kiwi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Apterygiformes; Apterygidae; Apteryx.
OX   NCBI_TaxID=8824 {ECO:0000313|Ensembl:ENSAOWP00000016946.1, ECO:0000313|Proteomes:UP000694424};
RN   [1] {ECO:0000313|Ensembl:ENSAOWP00000016946.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSAOWP00000016946.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   Ensembl; ENSAOWT00000019244.1; ENSAOWP00000016946.1; ENSAOWG00000011567.1.
DR   Proteomes; UP000694424; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.10.25.10:FF:000012; Delta-like protein; 1.
DR   FunFam; 2.40.10.10:FF:000068; transmembrane protease serine 2; 1.
DR   FunFam; 4.10.740.10:FF:000001; vitamin K-dependent protein S; 1.
DR   Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR050442; Peptidase_S1_coag_factors.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR   PANTHER; PTHR24278:SF25; COAGULATION FACTOR IX; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF57630; GLA-domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694424};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          35..81
FT                   /note="Gla"
FT                   /evidence="ECO:0000259|PROSITE:PS50998"
FT   DOMAIN          81..117
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          233..459
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   ACT_SITE        274
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT   ACT_SITE        314
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT   ACT_SITE        411
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT   DISULFID        107..116
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   469 AA;  52926 MW;  1BFEC3690FFBEF2B CRC64;
     VSKISLVIQF CHSSFTLSLF MRKDKAHEVL KVHKRANYFL EEIRPGNLER ECIEEKCSFE
     EAREIFHSQE KTMEFWFNYR GLNPCNTNPC KNGGVCKIRH YNYFCICPPK FGGDNCEREK
     LECWYKNGGC WHYCQDTERA FGVVCSCAKD YALHEDGKKC VQAGKVFNSR VIAVENAAGQ
     NQTAESTAGQ SEIGASQNVH KDLHQRHDGE NVSVGTWYTQ LNISTSEHSD SRITGGTACR
     RGHCPWQVML SFHRDIGFCG GSLISSRWVV TAAHCLDLVR PHHVTYVREM KEQKINVERS
     WTHPHYDSNN YNSDIALLYL SSEVVFNEYA IPICLPSPNL ATLLTAEGSV GMVSGWGATH
     HRGATLRFLQ EVRLPIVSMD TCQRSTEKLV TDNMFCAGYE AEAEDACKGD SGGPFAVSYH
     NTWFLLGIVS WGEGCAEKGK YGVYTRVSNY IPWIKEVVES VSDSEKILX
//
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