GenomeNet

Database: UniProt
Entry: A0A3Q4G9Q7_NEOBR
LinkDB: A0A3Q4G9Q7_NEOBR
Original site: A0A3Q4G9Q7_NEOBR 
ID   A0A3Q4G9Q7_NEOBR        Unreviewed;       506 AA.
AC   A0A3Q4G9Q7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Kunitz-type protease inhibitor 1-like {ECO:0000313|Ensembl:ENSNBRP00000005196.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000005196.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000005196.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   STRING; 32507.ENSNBRP00000005196; -.
DR   Ensembl; ENSNBRT00000005353.1; ENSNBRP00000005196.1; ENSNBRG00000003919.1.
DR   GeneTree; ENSGT00940000164935; -.
DR   OMA; HRNRFVC; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000003919; Expressed in zone of skin and 4 other cell types or tissues.
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; IPR022409; PKD/Chitinase_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; 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   SMART; SM00089; PKD; 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:UP000261580};
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..506
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018689923"
FT   TRANSMEM        449..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..114
FT                   /note="MANSC"
FT                   /evidence="ECO:0000259|PROSITE:PS50986"
FT   DOMAIN          249..299
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          378..428
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          481..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        322..334
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        329..347
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        341..356
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   506 AA;  55869 MW;  AE1BEA89B12DD5EB CRC64;
     XXXXPFHKPL TSALLVLIVR TVCSTGSDEF RRGHEDFVLY AEDAVKQGAV MLATASFYSE
     LECERACCGQ VHCNLALLEP SVPGEENRTC VLFNCVRRNR FACRFVTQSG YKSYVRDAVY
     RKYLAAPQKD GEYFQITTAQ TPVICGKKHP PVANAGRDVT IQPGETVMLN GTESVALSGA
     KIKDYRWSLE RGDSSVKIEE TNYPDQVQLS NLQTGSYVFK LTVNDSNGKS DDAKVTVLVL
     NPQQTSSYCQ APVKVGPCRA KFTRWRYNIT KGVCEMFVFG GCIGNENNFL SEQECLSACR
     GVTVSSQRSV TLPAAEVCGS PCGPDQLTCG NGCCLDRSME CDNVKQCSDG SDESQCHQLN
     QTLSLLLDID VNKKKAQCTE PPRTGPCRAK FPGWYYDPLD QKCHEFTYGG CDRNENNFPD
     DQTCSEYCKE VGGTHKFDMT SLSSSTGSIT LAVILSVAIL SLLAILAYCF LRARKRRTHR
     PVNTSPTHEA LSKEETSVYN STTKPM
//
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