ID M7BNY5_CHEMY Unreviewed; 461 AA.
AC M7BNY5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Kunitz-type protease inhibitor 1 {ECO:0000313|EMBL:EMP39626.1};
GN ORFNames=UY3_03222 {ECO:0000313|EMBL:EMP39626.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP39626.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(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; KB516251; EMP39626.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BNY5; -.
DR STRING; 8469.M7BNY5; -.
DR eggNOG; KOG4295; Eukaryota.
DR Proteomes; UP000031443; 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; cd00146; PKD; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR013980; MANSC_dom.
DR InterPro; IPR011106; MANSC_N.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
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; PF07502; MANEC; 1.
DR Pfam; PF18911; PKD_4; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 2.
DR SMART; SM00765; MANEC; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF57362; BPTI-like; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR PROSITE; PS50986; MANSC; 1.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..461
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004080191"
FT TRANSMEM 401..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..123
FT /note="MANSC"
FT /evidence="ECO:0000259|PROSITE:PS50986"
FT DOMAIN 145..235
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 240..290
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 323..373
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 461 AA; 51125 MW; C40C4AE88F050807 CRC64;
MASGRALLQA GLLIQLLRAA VLGQEGASFG ETCLADFTAG MPEFVLDSDA SVKNGATFLS
SPRVHRGKDC VRACCKQPAC NLALVQQAPH GEEDRIQACF LLDCLYEQAF VCKFARKVGF
LNYVRREVYD AYVDVRDQGS GDDKPPIARA GMDMKVQPQE PVLLRGTESS DDHGIVSYDW
KLLLGDTSVV VEKGEDQAEI SNLQEGQYVF QLTVTDSAGQ QDSSNITIMV LTAEQTEEFC
LAPSKVGRCR GSFPRWFYNP ASQQCERFTF GGCKANKNNY VREEECKLAC KNVQGSFGTR
AKPDALAFNK LRKINVTTEQ GHCVDLPDTG LCQESIPRWY YNPFTEKCDR FTYGGCEGNR
NNFEEEEECL KSCAGITKAD VIGQRWGAYG TQQAGLSAFE VAITVLLCIC IMVVLVIIGY
FFLKNRKRNS RRRQPTTATN STLSTTEDTE HLVYNSTTKP I
//
