ID W5MTR2_LEPOC Unreviewed; 1477 AA.
AC W5MTR2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011771.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011771.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR EMBL; AHAT01010398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01010399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000011771; -.
DR Ensembl; ENSLOCT00000011789.1; ENSLOCP00000011771.1; ENSLOCG00000009632.1.
DR eggNOG; KOG0546; Eukaryota.
DR GeneTree; ENSGT00940000158548; -.
DR InParanoid; W5MTR2; -.
DR OMA; DSHHKKR; -.
DR Proteomes; UP000018468; Linkage group LG9.
DR Bgee; ENSLOCG00000009632; Expressed in zone of skin and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR PANTHER; PTHR11071:SF257; NK-TUMOR RECOGNITION PROTEIN; 1.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 10..175
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 190..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..251
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..455
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..571
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..990
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1414
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1477 AA; 168717 MW; B14240B14F6FCDD4 CRC64;
MGIKDRPQCY FDVEINREPV GRIVFQLFSD ICPKTSKNFL CLCTGEKGTG KVTGKKLCYK
GSTFHRVVKS FMIQGGDFTE GNGRGGESIF GGYFEDENFS LKHDRAFLLS MANRGKDTNG
SQFFITTKMA PHLDGVHVVF GLVISGFEVI RQIENLKTDA ASRPYADVRV IDCGELITKS
NVLGNKKKVL SHSSDSSISS SDSSSSSSSS SESDSDSEEK YKSRKRKRQT KNKHSKRRRK
EGKRKENHTK RHPSSQRNYE HEAVDEEKEK DLNMKREKPV VRPEEIPPVP ENRFLLRRDM
PVQVSKPETA QLENSSIPND LKPAVTKSGR KIKGRGTMRY HTPPRSRSRS KSEDDGGSSE
TPPHWKEEMQ RTKTYKPPTG EKWSKGDKLN DHYSSRWDNR SASPWSRSWS HECFSDHSTE
RSSQPKRRRK EKKKAKHKKK SKKQKHSKRR KILKSKPKDS PLSENGSSLY SSRISKFSSH
RERRSRSFST SSRRLSREEW SDSDKVRHSS PSSRDSHSYT RSKTRSKSYS RSKSRTRSRS
SSRSRSVSRS RSQSRSRRRT ASRSPRKAKL NKSSKAKVDH PKLTTLKNEK VVKPEVSESV
PVLPLSDSPP PSRWKPGQKP WKPSYVRIQE IKAKTAPTNL VQAGHTVSSS KENDHSSHHS
QHKTSDSERS SDSRNYSNRS YKYSRRSRSR SSRSRSYSRS CSRSKTRSHS RSRSHSPLKS
ESLSSSYSRS DSYDSYKEYE RKKNSSERKE KHVSHVSSPE LKDSDNYVTN SKKRDVNKET
QSLSSSESTT DSENAEIDRK KQDDRESKIQ NTKSASLSEV DNVQTADPKH EEPNTGSVVE
EKKSKSEWDS DSDSSRKKTS VKDKSSEAQH IESHRTDEKD SVRKVFPMSK WDTESETEGE
TKKSNVSDSK LSSGKEEGEA SSESESEGLI SLNSKTSGNA SSENSDTNIK SVSKTPSVSV
VEGSNISTGS EKPKTKKKAK RKHKHKKRSS AKADSDRTKA KSKSKKAKRK TQKRKETFHW
QPPLEFGEEE DDEEEQNQQV QLKKNILKES AVKPNGGHSS SNSEDKESKF NTDKSQVQSK
EVCSSQSVSH SVKDIGELTK KKQKSKQSSE SCKKAENTEE MSNKCDATDT ERLLPKTPEK
PDSSDDTMEI CTPEPNTPER DHQISIICGI SEMSEIACQN SESSKINTES EYSLKTTPVE
KPKMQQRHSM PPSTLLVNNG PEEENVKNEV PGVVIDPKWK PLMGISNQQS VSTMAFGEIK
TLDHPELGEF KPHGLRIEIK SKSRVRPGSL FDEVRKTARL NQRPRNQESS SEERSPSVGN
KSKSRSRTRS LSKSRSVSSQ RTRSRTRSLS YSRSRTRSRS SSYSYRSRSY SRSRSRRRYS
RDRSLTRSST YRSYRSHSRT SSRSHSRSRS YDQRRRSRSH SYDSDYSRSS WSSRRRRSYS
YRKSRSYDRR SRSYRSYSRS DRSYSRHRSR SASSRYS
//