UniProt: A0A6P9D8X1

Database: UniProt
Entry: A0A6P9D8X1_PANGU

LinkDB:  A0A6P9D8X1_PANGU 
Original site:  A0A6P9D8X1_PANGU

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Ontology (7)   
   GO (7)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (24)   

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ID   A0A6P9D8X1_PANGU        Unreviewed;       371 AA.
AC   A0A6P9D8X1;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   08-OCT-2025, sequence version 2.
DT   28-JAN-2026, entry version 24.
DE   RecName: Full=Protein AMBP {ECO:0000256|ARBA:ARBA00018905};
GN   Name=AMBP {ECO:0000313|RefSeq:XP_034292152.2};
OS   Pantherophis guttatus (Corn snake) (Elaphe guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Pantherophis.
OX   NCBI_TaxID=94885 {ECO:0000313|Proteomes:UP001652622, ECO:0000313|RefSeq:XP_034292152.2};
RN   [1] {ECO:0000313|RefSeq:XP_034292152.2}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_034292152.2};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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}. Mitochondrion inner membrane
CC       {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004637}. Nucleus membrane
CC       {ECO:0000256|ARBA:ARBA00004126}. 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_034292152.2; XM_034436261.2.
DR   AlphaFoldDB; A0A6P9D8X1; -.
DR   GeneID; 117676641; -.
DR   KEGG; pgut:117676641; -.
DR   InParanoid; A0A6P9D8X1; -.
DR   Proteomes; UP001652622; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd22596; Kunitz_bikunin_1-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; 1.
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:ARBA00023180};
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW   Reference proteome {ECO:0000313|Proteomes:UP001652622};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          252..302
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          308..355
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          214..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  41552 MW;  233E8C4B13F61649 CRC64;
     MLEKHSCPVA APELPVGAEQ SRSAAAAMEP QVVLLICTAV FLSASSSPVA PADPIQIQKD
     FEEARVYGKW YAIALGTTCK WLKKYKERYL MGTLEVALGD TSKELSVTFT RLRQGTCSQA
     VGVYQKSSIP GKYHYYNSRW ETHIEGYVAR TNYDDYAFLA WKKNSSYGYT VTAQLYGRSP
     DLPEDLIEEF RQFSVALGIP EDSFFRLTET GECIPPQPEL NQQRDRRSTW DEEAGSADGS
     PLFGGGNRED FCLQPKDAGP CLGMELRYFY NTTSQNCERF YYGGCRGNQN NFPSERGCLQ
     TCRTEAACRL PIVPGEPCKD TFWAFDAKQG RCLTFQGCGG NANKFYLEKE CQEYCGLLPS
     DGEEFLRSSA L
//

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