ID A0A452H663_9SAUR Unreviewed; 608 AA.
AC A0A452H663;
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:ENSGAGP00000010006.1};
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:ENSGAGP00000010006.1, 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:ENSGAGP00000010006.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|ARBA:ARBA00001935};
CC -!- SIMILARITY: Belongs to the lysyl oxidase family.
CC {ECO:0000256|ARBA:ARBA00007492}.
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DR AlphaFoldDB; A0A452H663; -.
DR STRING; 38772.ENSGAGP00000010006; -.
DR Ensembl; ENSGAGT00000011488.1; ENSGAGP00000010006.1; ENSGAGG00000007859.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004720; F:protein-lysine 6-oxidase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001695; Lysyl_oxidase.
DR InterPro; IPR019828; Lysyl_oxidase_CS.
DR PANTHER; PTHR45817:SF8; LYSYL OXIDASE HOMOLOG 1; 1.
DR PANTHER; PTHR45817; LYSYL OXIDASE-LIKE-RELATED; 1.
DR Pfam; PF01186; Lysyl_oxidase; 1.
DR PRINTS; PR00074; LYSYLOXIDASE.
DR PROSITE; PS00926; LYSYL_OXIDASE; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW LTQ {ECO:0000256|ARBA:ARBA00022477};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..608
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019165347"
FT REGION 76..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 67737 MW; 803A2A3256E6AED5 CRC64;
MTACGLWDWW AVMGCGVFLL VHGQQPQSSN TDGNRWRQMI QWENNGRVYS LLNTGSEYVP
AGQESADGST RVLLADTPRS QSRRGHGNLR RQAPTLPVRA GSDTIRGQTR HPFGFGQVPE
NWREGPIGDS TSSQRIRPST SRQRQTSSSA AAVAASSSFS HSSFGQPSYP QFPFPQLPFG
NQHEPYEAQV SRGYDEGYLY YRSTGNGGGA VASAAAGVGV LYPLQPRAQY EEYGEDQNPY
RAQGYYPAPE RPYVAVPPQS QPADGLDRRY SHSLYHDTSA TAEQGFQDSY SAAQNQQPMG
QGIPSMDNLQ LSPGSPLGAS PRYGTDQRLG RYPPYGNVPL EPYVPPHNVE PQPPFRNLDP
YGSPRPEPYL PLRSPEAPQV ISDNQARVSV GSVYRPPQNG RGLPDLVPDP NYVQASTYIQ
RAHLYSLRCA AEEKCLASTA YTPEATDYDI RVLLRFPQRV KNQGTADFLP NRPRHNWEWH
SCHQHYHSMD EFSHYDLLDA PTGRKVAEGH KASFCLEDTT CDFGNLKRYA CTSHTQGLSP
GCYDTYNADI DCQWIDITDV QPGNYILKVQ VNPKYMVLES DFTNNVVRCN IHYTGRYVAT
TNCKIAQS
//
