ID R0J8K6_ANAPL Unreviewed; 513 AA.
AC R0J8K6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Kunitz-type protease inhibitor 1 {ECO:0000313|EMBL:EOA93291.1};
DE Flags: Fragment;
GN ORFNames=Anapl_16154 {ECO:0000313|EMBL:EOA93291.1};
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA93291.1, ECO:0000313|Proteomes:UP000296049};
RN [1] {ECO:0000313|Proteomes:UP000296049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749191; DOI=10.1038/ng.2657;
RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., Gan S.,
RA Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., Fairley S.,
RA Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., Lee T.,
RA Kim K.W., Sheng Z., An Y., Searle S., Herrero J., Groenen M.A.,
RA Crooijmans R.P., Faraut T., Cai Q., Webster R.G., Aldridge J.R.,
RA Warren W.C., Bartschat S., Kehr S., Marz M., Stadler P.F., Smith J.,
RA Kraus R.H., Zhao Y., Ren L., Fei J., Morisson M., Kaiser P., Griffin D.K.,
RA Rao M., Pitel F., Wang J., Li N.;
RT "The duck genome and transcriptome provide insight into an avian influenza
RT virus reservoir species.";
RL Nat. Genet. 45:776-783(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; KB747070; EOA93291.1; -; Genomic_DNA.
DR AlphaFoldDB; R0J8K6; -.
DR MEROPS; I02.007; -.
DR Proteomes; UP000296049; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd22623; Kunitz_HAI1_1-like; 1.
DR CDD; cd22624; Kunitz_HAI1_2-like; 1.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR013980; MANSC_dom.
DR InterPro; IPR011106; MANSC_N.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR46750; KUNITZ-TYPE PROTEASE INHIBITOR 1; 1.
DR PANTHER; PTHR46750:SF1; KUNITZ-TYPE PROTEASE INHIBITOR 1; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF07502; MANEC; 1.
DR Pfam; PF18911; PKD_4; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 2.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00765; MANEC; 1.
DR SUPFAM; SSF57362; BPTI-like; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50986; MANSC; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000296049};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..513
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004342638"
FT TRANSMEM 453..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..132
FT /note="MANSC"
FT /evidence="ECO:0000259|PROSITE:PS50986"
FT DOMAIN 250..300
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 375..425
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DISULFID 319..331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 326..344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 338..353
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EOA93291.1"
FT NON_TER 513
FT /evidence="ECO:0000313|EMBL:EOA93291.1"
SQ SEQUENCE 513 AA; 57473 MW; 2F2AE12B24F3D695 CRC64;
RGARMASRRP GPQSRLGVCL VLVAVAVVFG EEQETKPFGE TCLEDFTVGM PGLVLDTDAS
VQNGATFLSS PMVHRGRDCV RACCKDPACN LALVEQVPNS GEDHIQGCFL LNCLYEHSFV
CRFVRKAGFL NFLKKDVYDA YEAMPKHGSN DDRPPIARIG RDMRVQPGEP VMLRGADSTD
DRGIVSYEWK QILGDPSVEM KKQEEDQVEI SNLQVGTYVF QLTVTDTAQQ RDFTNITIVV
LNAEQTEEHC LTPKKVGWCR GSFPRWFYNP ALQQCEEFIF GGCKANKNNY LREEECKLAC
KNVKGSVGGR QMPVCNGNCQ APSFRCKDGC CIDAYLECDE TPDCADGSDE VYCEQYAREF
NRLQKINITR KQDHCVDLPN TGLCSESIPR WYYNPFSEKC DRFTYGGCGG NKNNFEEEGE
CMKSCSGITK ADAIGRRWES FEPQGAMLSA FEVVIAVLLG VCIMVVLVII GYFFLKNRRK
NSRRRQPTTA TNSTLSTTED TEHLFYNGAT KPV
//
