ID A0A164THD7_9CRUS Unreviewed; 1175 AA.
AC A0A164THD7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Kunitz domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=APZ42_025075 {ECO:0000313|EMBL:KZS10461.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS10461.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS10461.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS10461.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS10461.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZS10461.1}.
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DR EMBL; LRGB01001795; KZS10461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164THD7; -.
DR STRING; 35525.A0A164THD7; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 3.
DR CDD; cd00191; TY; 2.
DR CDD; cd00199; WAP; 1.
DR Gene3D; 4.10.75.10; Elafin-like; 2.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 3.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 3.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR InterPro; IPR008197; WAP_dom.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF217; PROTEIN CBG23496; 1.
DR Pfam; PF00014; Kunitz_BPTI; 3.
DR Pfam; PF00086; Thyroglobulin_1; 3.
DR Pfam; PF00095; WAP; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 3.
DR SMART; SM00211; TY; 3.
DR SMART; SM00217; WAP; 2.
DR SUPFAM; SSF57362; BPTI-like; 3.
DR SUPFAM; SSF57256; Elafin-like; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 3.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 3.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 3.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 3.
DR PROSITE; PS51390; WAP; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1080..1104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..80
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 83..149
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 391..448
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 454..505
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 498..558
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 627..677
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 684..734
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 869..941
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 805..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 121..128
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1175 AA; 127398 MW; 3B3FC9EB023C01DC CRC64;
MGSSCPSTHK CHLSPLGEFS VCCPKPRDVC FQDKLLGSCK ASILRYSFNE KRNRCEAFRY
TGCGGNMNNF ESERECKSVC PSLSTCEELR EKNLKMAEKF KKVVFTPKCN RANGDWEPVQ
CLEEVGICWC VDKDGEHIKG SLTRGTPTCG VRQARQRSID PPICADPTAV VHVCNKTICE
SKICLADPKA VCRVDPCGGC RHAFYNPATG RQVDCEAGLT KCQREVQTVL NSETWARQGG
PWNAQPLVVS TSSSPAYHYN LNGYSAPEED AEVLPDALLS SVTVYSSRLR RQVEEKEQAT
EAAMLDAMKE AAPSDLIAAM LKEAQTEEMD VASATETVFI EDTTPKETRS GKLLARPVDD
GLLDEVKNGF ESLDNVEEEA IQHRPLPALR DAIKPGFCPP VRSRTFLRVL AQFAGGAACA
DQCVSDADCA GPTRCCPGEC GSSCTHPVLL PTPLLPKPGA CPAPTHPFGC PADIEAVNDC
SSDADCSGRA KCCTNGCSST CTTPEENSSG PLMMSISPPV CTLKGDYARE QSQGEFSWCV
DTTGQPIDDS FTRGSVRCSP NGAVLEQRAL GPICPDPSVQ PTVCRDQCLH ARCPFHPDAL
CVADPCNNCK VSFIDPQDNP LECVDRCSQP AETGHCRALF PRYFYNSSSK ACEEFIYGGC
EGNENNFESL QECSQHCERP VNVCELPKEP GMCRASFPRW AYNPETQQCE KFSFGGCGGN
ANNFYSYQQC ASRCPDMVLC PQQSPLGEMT SCSRNQACAE KTCPNHPEAA CSVDPCTCTP
VFLDAEGNAI ECLPSSMLEV EPRHAKDFES TTASTSTTTT TTTTTEASTT STTKATTTTT
TSTTTTTPTT TTATPSPVLR GKALNHPHYT RCQKMRQNQL KQGGAGELIP ECDHLGRFQP
IQCLPAKSSN GGHPIVNCWC VDEAGNQVAN TTQFVRGEQT CRLVPIMAVA MTLGFPAMDH
AQGVMEKEVR QQVGEILNGL SARTMEPTLK VKSRNDGTVL TFTLVGDNKI DVASHLEDMV
KSGHLALEMD GHSMPAESTS SKFYLKLDST LKEASKAEAV DRSLETREIL TQALDIEAPY
LAIIVVLSVL ASILVCGLII GLVLHRRRTT GTYPKNSGST LASPPKPNKH NLDKSDVVPR
GFPRVGINPS DVVQTPQLSP TVPRSKRQTR NAEAW
//
