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FGL1L_CHICK
ID   FGL1L_CHICK             Reviewed;         281 AA.
AC   O93526; F1P1D2;
DT   22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2015, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Fibrinogen-like protein 1-like protein {ECO:0000305};
DE   AltName: Full=Cytidine deaminase {ECO:0000303|PubMed:9792440};
DE            Short=CDD {ECO:0000312|EMBL:AAC64000.1};
DE   Flags: Precursor;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-140 AND GLU-143.
RC   TISSUE=Small intestine;
RX   PubMed=9792440; DOI=10.1515/bchm.1998.379.8-9.1075;
RA   Anant S., Yu H., Davidson N.O.;
RT   "Evolutionary origins of the mammalian apolipoproteinB RNA editing enzyme,
RT   apobec-1: structural homology inferred from analysis of a cloned chicken
RT   small intestinal cytidine deaminase.";
RL   Biol. Chem. 379:1075-1081(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
CC   -!- FUNCTION: Shows a cytidine deaminase activity on 2'-deoxycytidine (in
CC       vitro), however shows no RNA editing activity (in vitro).
CC       {ECO:0000269|PubMed:9792440}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.22 uM for 2'-deoxycytidine {ECO:0000269|PubMed:9792440};
CC   -!- TISSUE SPECIFICITY: Expressed in smal intestine, colon and lung.
CC       {ECO:0000269|PubMed:9792440}.
CC   -!- CAUTION: Although in PubMed:9792440 a cytidine deaminase activity has
CC       been shown in vitro, it would be the first time that a member of this
CC       family that contains a fibrinogen C-terminal domain signature shows an
CC       enzymatic activity. And it is surprising that this protein that shows
CC       an in vitro cytidine deaminase activity does not have the cytidine and
CC       deoxycytidylate deaminases domain signature.
CC       {ECO:0000305|PubMed:9792440}.
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DR   EMBL; AF059262; AAC64000.1; -; mRNA.
DR   EMBL; AADN03012049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; O93526; -.
DR   SMR; O93526; -.
DR   STRING; 9031.ENSGALP00000022348; -.
DR   PaxDb; O93526; -.
DR   VEuPathDB; HostDB:geneid_395773; -.
DR   eggNOG; KOG2579; Eukaryota.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004126; F:cytidine deaminase activity; IDA:UniProtKB.
DR   GO; GO:0047844; F:deoxycytidine deaminase activity; IDA:UniProtKB.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 3.90.215.10; -; 1.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Reference proteome; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..281
FT                   /note="Fibrinogen-like protein 1-like protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000433469"
FT   DOMAIN          34..246
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   REGION          260..281
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        43..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   DISULFID        201..213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   MUTAGEN         140
FT                   /note="H->R: Abolishes cytidine deaminase activity."
FT                   /evidence="ECO:0000269|PubMed:9792440"
FT   MUTAGEN         143
FT                   /note="E->Q: Abolishes cytidine deaminase activity."
FT                   /evidence="ECO:0000269|PubMed:9792440"
FT   CONFLICT        105
FT                   /note="N -> D (in Ref. 1; AAC64000)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="G -> R (in Ref. 1; AAC64000)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="T -> I (in Ref. 1; AAC64000)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281
FT                   /note="Missing (in Ref. 1; AAC64000)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  31298 MW;  942D8BA9035F0C71 CRC64;
     MGLQAGTRQL HGNLILLPVA VVMLLLCTSP VCATASVGLP ADCSRLTSSS PSGVYVIQPA
     QSPPRVVWCD MDTEGKGWTV VQRNTYSTEI TWKESWTTYK YGFGNVQGDH WLGTEYLHLL
     TQQGTYKVRF VVRDKANVTH YAEYDIFRVE SESSGYPLRL GRLLSSGKDY LTSYYSSYGG
     IHDNMKFSTV DKDQDQHSGN CASSYGGWWY DRCQNVLLNG KKYILWPEIC PRVTACRPSS
     WSNPPMCADC ARGWGSATIP SRSPSLPSPI TATHTVRNQL Q
 
 
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