ID A0A452INT6_9SAUR Unreviewed; 483 AA.
AC A0A452INT6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000029632.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000029632.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000029632.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR AlphaFoldDB; A0A452INT6; -.
DR STRING; 38772.ENSGAGP00000029632; -.
DR Ensembl; ENSGAGT00000033646.1; ENSGAGP00000029632.1; ENSGAGG00000021395.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00104; KAZAL_FS; 1.
DR Gene3D; 2.40.10.120; -; 2.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 4.10.40.20; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF13; SERINE PROTEASE HTRA1; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00121; IB; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019159344"
FT DOMAIN 31..101
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51323"
FT DOMAIN 84..145
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
SQ SEQUENCE 483 AA; 51990 MW; D0E6473644AC2530 CRC64;
MLLWLSWAGG CCLLLLLPGS AAEPARRYDE RAAGCSERCD RARCPAVPAD CAGGEALDAC
GCCPVCAAQE GEPCGGPAGE PPCGEGLQCR KRAKAGLCVC TSSEPVCGSD ARTYGNLCQL
RAASRRSERL QQPPVIAIQR GACGQGQEDP NSLRHKYNFI ADVVEKIAPA VVHIELFRKL
PFTKREVPVA SGSGFIVSED GLIVTNAHVV TNKHRVKVEL KNGATYEAKI KDVDEKADIA
LIKIDTQGKL PVLLLGRSAD LRPGEFVVAI GSPFSLQNTV TTGIVSTTQR GGKELGLRNS
DMDYIQTDAI INYGNSGGPL VNLDGEVIGI NTLKVTAGIS FAIPSDKIKK FLTESHDRQA
KGKAITKKKY IGIRMMSLSP SKAKELKEHH KDFPDVVSGA YIIEVIPDTP AEDGEVIGIN
TLKVTAGISF AIPSDKIKKF LTESHDRQAK GIVLYYFLKM GTCHTIGNQH QNIWEKTSNY
LCV
//
