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Database: UniProt
Entry: A0A4D9E9T4_9SAUR
LinkDB: A0A4D9E9T4_9SAUR
Original site: A0A4D9E9T4_9SAUR 
ID   A0A4D9E9T4_9SAUR        Unreviewed;       545 AA.
AC   A0A4D9E9T4;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Protein quaking {ECO:0000313|EMBL:TFK07961.1};
GN   ORFNames=DR999_PMT09162 {ECO:0000313|EMBL:TFK07961.1};
OS   Platysternon megacephalum (big-headed turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Platysternidae; Platysternon.
OX   NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK07961.1, ECO:0000313|Proteomes:UP000297703};
RN   [1] {ECO:0000313|EMBL:TFK07961.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK07961.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK07961.1};
RA   Gong S.;
RT   "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TFK07961.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK07961.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK07961.1};
RA   Gong S.;
RT   "The genome sequence of big-headed turtle.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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:TFK07961.1}.
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DR   EMBL; QXTE01000075; TFK07961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4D9E9T4; -.
DR   STRING; 55544.A0A4D9E9T4; -.
DR   Proteomes; UP000297703; 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; 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; 1.
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; PTHR46876; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 11; 1.
DR   PANTHER; PTHR46876:SF1; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 11; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF07502; MANEC; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00131; KU; 1.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00765; MANEC; 1.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
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:UP000297703};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..545
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020023521"
FT   TRANSMEM        496..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          63..147
FT                   /note="MANSC"
FT                   /evidence="ECO:0000259|PROSITE:PS50986"
FT   DOMAIN          388..438
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          165..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        280..292
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        287..305
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        299..314
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   545 AA;  58256 MW;  2AC9718FB048B647 CRC64;
     MASRLLLLLA ALCGRAPGGE VAAPLAELRS QISGVESLLE EFRRQLQPDE AGRGSCRGGA
     FSARPDAIIR TKDSLAAGAT FLRAPAAVAG WRQCLQACCA EPRCSLAVVQ RARPPGEPGA
     LSCYLFNCTY RGRAVCRFAP HRGYSSYSLG PANLTQLLAH GPRGSPLPAL TQAAENDKPP
     HSKAGQDIVL QSPVDWVILD GRESLDDHGI IQYEWTLLQG DSSVDIKVPQ PGTLKLSHLQ
     EGVYIFQLTV TDTAGQKSSD NISVTVLPMV HSALGCTGVC SRYQFICDDG CCIDITFACD
     GVEQCPDGSD EAFCQNFSPG RKTVTHAAIS TAQQRIVGLT KDADNSVENT QKNTIRNQPL
     LSLDADKSNQ SLSQGPKKQI SGFIPEQCLV PPAAGPCKGH FPRWHFDISS GTCLHFIYGG
     CKGNENNFLQ ESDCLSECVE IHGAISQQTA TDPSSQSNSE PANSSSGKRT GKNENGIVVS
     KSDQAAGEHP VPETGAVLPL ALGLAITALL LLMVACRLRL VRQKLKKARP ITSEESDYLI
     NGMYL
//
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