ID A4IIZ2_XENTR Unreviewed; 984 AA.
AC A4IIZ2;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=LOC100125091 protein {ECO:0000313|EMBL:AAI36212.1};
GN Name=LOC100125091 {ECO:0000313|EMBL:AAI36212.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI36212.1};
RN [1] {ECO:0000313|EMBL:AAI36212.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000313|EMBL:AAI36212.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718}.
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DR EMBL; BC136211; AAI36212.1; -; mRNA.
DR RefSeq; NP_001096472.1; NM_001103002.1.
DR AlphaFoldDB; A4IIZ2; -.
DR AGR; Xenbase:XB-GENE-1011831; -.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd03122; alpha_CARP_receptor_like; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR041887; Alpha_CARP_receptor-type.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF134; CARBONIC ANHYDRASE 15; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS50853; FN3; 1.
PE 2: Evidence at transcript level;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..984
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002669716"
FT DOMAIN 36..300
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 314..412
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 836..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 109059 MW; 550B43535DE4FA7F CRC64;
MLNPRCFLAC LQLLSVWQVG LPFSYYRQQR KLTEEIDWSY TETLNQENWV KKYPVCNGAK
QSPINIDEDL TQLNTNLKKL HFEGWDKESS ELTLIRNTGK TVEINLTDDY YLSGGALDSQ
YKASRITFHW GKCNATSDGS EHSLEGQKFP LEMQIFCFNH NEFKNIDEAI SGNGKIKALS
ILFKVGQEDN VHYNEIIDGV DNVHRFGTKV ALGPFILSNL LPDYTDKYYT YNGSLTTPPC
SETVEWIVFK DTVTISESQL EMFCEILTMQ QSGYVMVMDY LQNNYRHQQY KFSGQVFSSY
TGTEEIPEPV CSSEPEDVRA DSKNNTSLLI TWRRPRVVYD AVIERYLVFY QHLEGEDQTK
HEYLTDGYQD LGAIIYNLVP NTSYVLQVVA ICTNGLYGKR SDQVIVDMTV DAQGTDQFTD
FTETEEDIED SEEVEEENEN KSTRIFLSTV SSTNQKQAQG GQATTSSYSE EITYVTTVKT
EGDKLKEHRD VLKAYLYPTL QTTTKTMSDT TVGSSRKSVE HAVMPQSVSE ATTYLSKDFK
SRVEIWMLNI SDSTQSVTEE DEQTSADSEL HTTTTSWKRR ILIPTRNPKP VSNHTTDTTP
PTVSATFVSE ITPQGNIVSS DINDYFSSTS EDIAKVTAPV TEFDLYKIST STSTSNVPVV
SEEQHPTDSV SLHIDELLST SLSSGATVLQ ATASSLEEMN KATLPGKEML PVSNTTFSTP
EALLESVSAS FGHHDSESSV SEVLSQATLS QTTQPVSNAG FPKSESPSTL TMLTATSQTS
SDILPTVSSD AKMGPSVVDD GFIIASTYST SHTETQGNVV ADNSSFVHRE MLKNKTFSEH
SEQSEDGSAF STAAADNNID SDMEGESYLS TTMPMSSTGQ KHIPFTAPET HIQTLNTLLE
NTSESRSWAV LTDEESGSGP STSDSLSDNE TSTDFNFSDI NDRDKDYEVA IQPGKADLTP
GSEMTSPPSV TSERSPVVNV SEAG
//