ID A0A1S2ZZ15_ERIEU Unreviewed; 352 AA.
AC A0A1S2ZZ15;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Protein AMBP {ECO:0000256|ARBA:ARBA00018905};
GN Name=AMBP {ECO:0000313|RefSeq:XP_007526812.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007526812.1};
RN [1] {ECO:0000313|RefSeq:XP_007526812.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Kunitz-type serine protease inhibitor. Has high catalytic
CC efficiency for F10/blood coagulation factor Xa and may act as an
CC anticoagulant by inhibiting prothrombin activation. Inhibits trypsin
CC and mast cell CMA1/chymase and tryptase proteases.
CC {ECO:0000256|ARBA:ARBA00029383}.
CC -!- SUBUNIT: Monomer. Also occurs as a complex with tryptase in mast cells.
CC {ECO:0000256|ARBA:ARBA00029474}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm,
CC cytosol {ECO:0000256|ARBA:ARBA00004514}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004637}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004617}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004617}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the calycin
CC superfamily. Lipocalin family. {ECO:0000256|ARBA:ARBA00008238}.
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DR RefSeq; XP_007526812.1; XM_007526750.2.
DR AlphaFoldDB; A0A1S2ZZ15; -.
DR STRING; 9365.ENSEEUP00000009394; -.
DR GeneID; 103116802; -.
DR CTD; 259; -.
DR eggNOG; KOG4295; Eukaryota.
DR InParanoid; A0A1S2ZZ15; -.
DR OrthoDB; 3558236at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd22596; Kunitz_bikunin_1-like; 1.
DR CDD; cd22597; Kunitz_bikunin_2-like; 1.
DR CDD; cd19418; lipocalin_A1M-like; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
DR InterPro; IPR002968; A1-microglobln.
DR InterPro; IPR029856; AMBP.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR46676; PROTEIN AMBP; 1.
DR PANTHER; PTHR46676:SF1; PROTEIN AMBP; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01215; A1MCGLOBULIN.
DR PRINTS; PR00759; BASICPTASE.
DR PRINTS; PR00179; LIPOCALIN.
DR SMART; SM00131; KU; 2.
DR SUPFAM; SSF57362; BPTI-like; 2.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chromophore {ECO:0000256|ARBA:ARBA00022991};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..352
FT /note="Protein AMBP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010342478"
FT DOMAIN 231..281
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 287..337
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 352 AA; 39284 MW; 9CC00B5858707306 CRC64;
MRILEVLIGL LTSCLAVSAG PVPTSPGSIQ VQENFDLSRI YGKWFHVAIG STCPWLKRFK
DKMSVSTLVL GAGTSENEIS TTNTRWRKGI CEEISGAYEK TDTKGKFLYH KSRWNITIES
YVVHTNYDEY VIIVTKKFSR HHGDTITAKL YGRESHLRES LLEDFREFAL GLGIPEDSIF
TMADRGECVS GEREPESTLG LRFRRAVLPQ EDEGSGAEQQ MADFNKKEDS CQLSHAEGPC
LGMVKRYFYN GSSMACETFQ YGGCLGNGNN FVSEKECLQT CRTVEACNLP IVTGPCKGFF
MLWAFDAVQG KCIQFTYGGC KGNGNQFYSE KECKEYCGVP GEGDEELLRV SS
//
