ID H2SB93_TAKRU Unreviewed; 502 AA.
AC H2SB93;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Kunitz-type protease inhibitor 1-like {ECO:0000313|Ensembl:ENSTRUP00000009671.2};
GN Name=LOC101073645 {ECO:0000313|Ensembl:ENSTRUP00000009671.2};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000009671.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000009671.2, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000009671.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR RefSeq; XP_011616911.1; XM_011618609.1.
DR AlphaFoldDB; H2SB93; -.
DR STRING; 31033.ENSTRUP00000009671; -.
DR Ensembl; ENSTRUT00000009726.3; ENSTRUP00000009671.2; ENSTRUG00000004077.3.
DR GeneID; 101073645; -.
DR KEGG; tru:101073645; -.
DR eggNOG; KOG4295; Eukaryota.
DR GeneTree; ENSGT00940000164935; -.
DR InParanoid; H2SB93; -.
DR OMA; HRNRFVC; -.
DR OrthoDB; 2909633at2759; -.
DR TreeFam; TF325867; -.
DR Proteomes; UP000005226; Chromosome 16.
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 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:UP000005226};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..502
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017307710"
FT TRANSMEM 445..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..118
FT /note="MANSC"
FT /evidence="ECO:0000259|PROSITE:PS50986"
FT DOMAIN 238..288
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 367..417
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DISULFID 311..323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 318..336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 330..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 502 AA; 54880 MW; 76D9F6E48EE7162A CRC64;
MSPCSLSSVL LPLLLLRCAA AEPTAQCNSA FRSGPEDFVL DSEDAVMEGA AILDSAQVPS
ADACQSLCCE RAHCNLALLD PRFRGAEDAR NFTCVLFNCI HRNRFVCRFV NLVGYRSFIR
ESVYLKHLQG PDGDGKQVPP IANAGRDVVV QPGTLVVLNG IESLPLGGAH ITDYHWALQS
GNNKVSIEQT DLPDQVHVSG LQPGSYIFQL TVTDSNHQSD AANVSVLVLS PEQSSSFCQA
PVKVGPCRAA FPRWWYNSST GDCERFTFGG CKGNNNNFLS KEECLSACKG VTETSERRVT
VPTARVCGSL CSPSQLTCGA GCCLHKSLEC DGVKHCSDGS DENHCSELNQ TFSRLLEIDV
NRKKARCSEP PHTGPCRASF TRWYYNPLDR KCARFTYGGC DANDNNFEEE PKCEESCSGV
TEQSVYFRGL FERFEKEEES ESGNIALAVL LAVAILALLA ILTYCFLKSR RKRSHRPVAT
GPAHVALSEQ DTLVYNSTTK PI
//
