ID L5K9L7_PTEAL Unreviewed; 353 AA.
AC L5K9L7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Protein AMBP {ECO:0000256|ARBA:ARBA00018905};
GN ORFNames=PAL_GLEAN10009842 {ECO:0000313|EMBL:ELK08235.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK08235.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 EMBL; KB030911; ELK08235.1; -; Genomic_DNA.
DR RefSeq; XP_006917168.1; XM_006917106.1.
DR AlphaFoldDB; L5K9L7; -.
DR STRING; 9402.L5K9L7; -.
DR MEROPS; I02.005; -.
DR GeneID; 102879765; -.
DR KEGG; pale:102879765; -.
DR CTD; 259; -.
DR eggNOG; KOG4295; Eukaryota.
DR InParanoid; L5K9L7; -.
DR OrthoDB; 3558236at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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:UP000010552};
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..353
FT /note="Protein AMBP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003968993"
FT DOMAIN 232..282
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 288..338
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 353 AA; 39473 MW; 4D53CF94490C96E0 CRC64;
MQSLGALPLL LAACVVVSTN PVPTLPDDIQ VQENFDISRF YGKWFHVAMG STCPWLLKLK
DRLTISTLEL KRGPTERQIS TTSTRWRKGV CEEISGTYEK TDIDGKFLYR KSKWNITIES
YVVHTNYDEY AIILSKKLFN RHHGPTITAK LYGREQQLRE SLLEEFRETA LGVGIPEDSI
FTMADRGECV PGEQEPEPTS LPRARRAVLP QEEEGSGAGQ PAADFDKKED SCQLGYAEGP
CLGMVRRYFY NGSSMACETF QYGGCLGNGN NFASEKECLQ TCRTVAACNL PIVRGPCHSY
NQLWAFDAVQ GKCVLFTYGG CQGNGNKFYS EKECKEYCGV PGDGDEELLR FSN
//
