ID G1NGK7_MELGA Unreviewed; 709 AA. AC G1NGK7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 73. DE SubName: Full=Transglutaminase 4 {ECO:0000313|Ensembl:ENSMGAP00000012230.1}; GN Name=TGM4 {ECO:0000313|Ensembl:ENSMGAP00000012230.1}; OS Meleagris gallopavo (Wild turkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Meleagridinae; Meleagris. OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000012230.1, ECO:0000313|Proteomes:UP000001645}; RN [1] {ECO:0000313|Ensembl:ENSMGAP00000012230.1, ECO:0000313|Proteomes:UP000001645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475; RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A., RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K., RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C., RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A., RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P., RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T., RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M., RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D., RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C., RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J., RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P., RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X., RA Zhang Y., Reed K.M.; RT "Multi-platform next-generation sequencing of the domestic turkey RT (Meleagris gallopavo): genome assembly and analysis."; RL PLoS Biol. 8:E1000475-E1000475(2010). RN [2] {ECO:0000313|Ensembl:ENSMGAP00000012230.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) 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. {ECO:0000256|PIRSR:PIRSR000459-2}; CC -!- SIMILARITY: Belongs to the transglutaminase superfamily. CC Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_003207295.1; XM_003207247.3. DR AlphaFoldDB; G1NGK7; -. DR Ensembl; ENSMGAT00000013118.2; ENSMGAP00000012230.1; ENSMGAG00000011669.3. DR GeneID; 100541357; -. DR KEGG; mgp:100541357; -. DR CTD; 7047; -. DR GeneTree; ENSGT01050000244939; -. DR InParanoid; G1NGK7; -. DR OrthoDB; 5344745at2759; -. DR Proteomes; UP000001645; Chromosome 6. DR Bgee; ENSMGAG00000011669; Expressed in heart and 17 other cell types or tissues. DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro. DR Gene3D; 2.60.40.10; Immunoglobulins; 3. DR Gene3D; 3.90.260.10; Transglutaminase-like; 1. 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; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1. DR PANTHER; PTHR11590:SF70; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE 4; 1. DR Pfam; PF00927; Transglut_C; 1. 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; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF49309; Transglutaminase, two C-terminal domains; 2. DR PROSITE; PS00547; TRANSGLUTAMINASES; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR000459-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001645}. FT DOMAIN 259..352 FT /note="Transglutaminase-like" FT /evidence="ECO:0000259|SMART:SM00460" FT ACT_SITE 267 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 326 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 349 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT BINDING 389 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 391 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 441 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 446 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" SQ SEQUENCE 709 AA; 79055 MW; BB52AFD2251623DB CRC64; MSQDRDLKVT KVDFLKSQNS VQHHTDAYNT SNLVVRRGQP FLVQLTLSRE LRASDKLSLH FSIGEKPKEP TGTLMSLNPR STRNVSGWQI SIVKSSGTEC TLSVTSAPNA AVGIYGLIVK TGPNVYKPEK NTVYLLFNPW CEGDIVFLSN EAERKEYVLN DTGYIYVGSA FNIHSKPWNF GQFEESILDA CMYLLDKSKL KMSSRRDPVV VSRAMSALVN ANDDSGVVLG NWSGKYENGT SPMAWIGSVA ILQQYYKTKK PVSYGQCWVF SGVLTTVMRC LGIPARSVSN FNSAHDTDEN LRVDVYLNEK GEKLKWMSSD SVWNFHVWND VWMKRKDLPS GFDGWQAIDA TPQEQSQGIF QCGPCPVKAV KDGDVYLPYD SKFVYAEVNA DKVYWRVKEE NGRNKYTKLG VESQSIGANI STKAVGQNRR EDITWQYKFP EGSSEERASM KRAVSYLQPS GMTPRSRFAA VPLDVNLRNA GDEDTIQNEV VPKSGVQLEI TNEKPLCPGN PIEVVITVKS TVAGSWTVDL ASSCQLQSYT GKVHANLGYI KQTVKVEGQS EVRVPLKIMP EAYMKALATV DDEEHVHVTA IAEIQGTPEK LTKEVSLSFE YPPIQVQMPE TAQVNKDFTC AFIFKNKLNV PLDNCKLMVE GLGIFKMATF DEGDIQPGRI IKSEVICTPT RVGEKKIVAR LTSNQVKDIS VEKGIMVTH //