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Database: UniProt
Entry: G1PRQ2_MYOLU
LinkDB: G1PRQ2_MYOLU
Original site: G1PRQ2_MYOLU 
ID   G1PRQ2_MYOLU            Unreviewed;       705 AA.
AC   G1PRQ2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   10-OCT-2018, entry version 45.
DE   SubName: Full=Coagulation factor XIII A chain {ECO:0000313|Ensembl:ENSMLUP00000013831};
GN   Name=F13A1 {ECO:0000313|Ensembl:ENSMLUP00000013831};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000013831, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000013831, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
RA   Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
RA   Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
RA   Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
RA   Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
RA   Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
RA   Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
RA   Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
RA   Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
RA   Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
RA   Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
RA   Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
RA   Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
RA   Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
RA   Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
RA   Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29
RT   mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000013831}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000459-2};
CC       Note=Binds 1 Ca(2+) ion per subunit.
CC       {ECO:0000256|PIRSR:PIRSR000459-2};
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DR   EMBL; AAPE02037929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAPE02037930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000013831; -.
DR   Ensembl; ENSMLUT00000015183; ENSMLUP00000013831; ENSMLUG00000015173.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   GeneTree; ENSGT00760000119108; -.
DR   InParanoid; G1PRQ2; -.
DR   OMA; CEEDAVY; -.
DR   OrthoDB; EOG091G030K; -.
DR   TreeFam; TF324278; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:Ensembl.
DR   GO; GO:0072378; P:blood coagulation, fibrin clot formation; IEA:Ensembl.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:Ensembl.
DR   Gene3D; 2.60.40.10; -; 3.
DR   Gene3D; 3.90.260.10; -; 1.
DR   InterPro; IPR034810; Factor_XIII_A.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR038765; Papain_like_cys_pep_sf.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR036985; Transglutaminase-like_sf.
DR   InterPro; IPR023608; Transglutaminase_animal.
DR   InterPro; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR036238; Transglutaminase_C_sf.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   PANTHER; PTHR11590:SF42; PTHR11590:SF42; 1.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   PIRSF; PIRSF000459; TGM_EBP42; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF49309; SSF49309; 2.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001074};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT   DOMAIN      280    373       TGc. {ECO:0000259|SMART:SM00460}.
FT   ACT_SITE    288    288       {ECO:0000256|PIRSR:PIRSR000459-1}.
FT   ACT_SITE    347    347       {ECO:0000256|PIRSR:PIRSR000459-1}.
FT   ACT_SITE    370    370       {ECO:0000256|PIRSR:PIRSR000459-1}.
FT   METAL       410    410       Calcium. {ECO:0000256|PIRSR:PIRSR000459-
FT                                2}.
FT   METAL       412    412       Calcium. {ECO:0000256|PIRSR:PIRSR000459-
FT                                2}.
FT   METAL       459    459       Calcium. {ECO:0000256|PIRSR:PIRSR000459-
FT                                2}.
FT   METAL       464    464       Calcium. {ECO:0000256|PIRSR:PIRSR000459-
FT                                2}.
SQ   SEQUENCE   705 AA;  80326 MW;  6C1BC549032139FE CRC64;
     PTSPLNRVLP NRPSCFNYLH VTTVHLFKEP WDTNKVDHHT DKYNNNKLIV RRGQSFYIQI
     EFNRPYNPRK DFFRVEYVIG RYPQENKGTY IPVPVVRELR SGKWGAKVIS TEDRSVRLSI
     QSSPECIVGK FRMYIAVWTP YGILRTSRNP ETDTYILFNP WCEEDAVYLE DEREREEYVL
     NDIGVIFYGD FNNIKSRSWS YGQFEDGILD ACLHLMDKAQ MDLSGRGNPI KVSRVGSAMV
     NSKDDEGVLV GSWDNVYAYG VPPSAWTGSI DILLEYQSSQ NPVRYGQCWV FAGVFNTFLR
     CLGIPARVVT NYFSAHDNDA NLQMDIFLQE DGNVNSKLTK DSVWNYHCWN EAWMTRPDLP
     VGFGGWQAVD STPQENSDGM YRCGPASVQA IKHGHVCFQF DAPFVFAEVN SDLVYITAKK
     DGTHVVEAVD TTHVGKLIVT KQIGGDGMND ITDNYKFPEG QKEERLALET ALMYGVKKPL
     NTEGIVKQRS DVDMDFVVEN AVLGKDFKVT ITFQNNSPKA YTISAYLSGN ITFYTGVSKE
     EFKNETFEVA LDPLSFKKEE VLVRASEYMG QLLEQASLHF FVTARVNETG DILAKQKSTV
     LTIPTITIKV RGAQMVGSDM VVTVEFTNPL KESLKNVWIR LEGPGVIKPM RKMFREIRPN
     STVQWEEVCR PWVSGLRKLM ASMTSDSLRH VYGELDLQIQ RQRTV
//
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