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Database: UniProt
Entry: A4IIZ2_XENTR
LinkDB: A4IIZ2_XENTR
Original site: A4IIZ2_XENTR 
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
//
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