ID TGM3L_HUMAN Reviewed; 706 AA. AC O95932; Q5JXU4; Q5JXU5; Q719M2; Q719M3; Q9Y4U8; DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2005, sequence version 3. DT 04-NOV-2008, entry version 72. DE RecName: Full=Protein-glutamine gamma-glutamyltransferase 6; DE EC=2.3.2.13; DE AltName: Full=Transglutaminase-3-like; DE Short=TGase-3-like; DE AltName: Full=Transglutaminase Y; GN Name=TGM6; Synonyms=TGM3L; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT VAL-58. RC TISSUE=Lung; RA Thomas H., Aeschlimann D.; RT "A novel transglutaminase expressed in the nervous system."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). CC -!- FUNCTION: Catalyzes the cross-linking of proteins and the CC conjugation of polyamines to proteins (By similarity). CC -!- CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N(5)- CC alkylglutamine + NH(3). CC -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long; CC IsoId=O95932-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=O95932-2; Sequence=VSP_015103, VSP_015104; CC -!- SIMILARITY: Belongs to the transglutaminase superfamily. CC Transglutaminase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF540969; AAQ10751.1; -; mRNA. DR EMBL; AF540970; AAQ10752.1; -; mRNA. DR EMBL; AL049650; CAI22576.1; -; Genomic_DNA. DR EMBL; AL031678; CAI22576.1; JOINED; Genomic_DNA. DR EMBL; AL049650; CAI22577.1; -; Genomic_DNA. DR EMBL; AL031678; CAI22577.1; JOINED; Genomic_DNA. DR EMBL; AL031678; CAI22900.1; -; Genomic_DNA. DR EMBL; AL049650; CAI22900.1; JOINED; Genomic_DNA. DR EMBL; AL031678; CAI22901.1; -; Genomic_DNA. DR EMBL; AL049650; CAI22901.1; JOINED; Genomic_DNA. DR RefSeq; NP_945345.2; -. DR UniGene; Hs.452039; -. DR HSSP; Q08188; 1L9M. DR Ensembl; ENSG00000166948; Homo sapiens. DR GeneID; 343641; -. DR KEGG; hsa:343641; -. DR NMPDR; fig|9606.3.peg.19725; -. DR HGNC; HGNC:16255; TGM6. DR PharmGKB; PA38098; -. DR HOGENOM; O95932; -. DR HOVERGEN; O95932; -. DR DrugBank; DB00130; L-Glutamine. DR NextBio; 98594; -. DR ArrayExpress; O95932; -. DR CleanEx; HS_TGM6; -. DR GermOnline; ENSG00000166948; Homo sapiens. DR GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR008958; Transglutaminase_C. DR InterPro; IPR013808; Transglutaminase_CS. DR InterPro; IPR001102; Transglutaminase_N. DR InterPro; IPR002931; Trnsglumase_like. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3. DR Pfam; PF00927; Transglut_C; 2. DR Pfam; PF01841; Transglut_core; 1. DR Pfam; PF00868; Transglut_N; 1. DR SMART; SM00460; TGc; 1. DR PROSITE; PS00547; TRANSGLUTAMINASES; 1. PE 2: Evidence at transcript level; KW Acyltransferase; Alternative splicing; Calcium; Metal-binding; KW Polymorphism; Transferase. FT CHAIN 1 706 Protein-glutamine gamma- FT glutamyltransferase 6. FT /FTId=PRO_0000213715. FT ACT_SITE 274 274 By similarity. FT ACT_SITE 333 333 By similarity. FT ACT_SITE 356 356 By similarity. FT METAL 396 396 Calcium (By similarity). FT METAL 398 398 Calcium (By similarity). FT METAL 445 445 Calcium (By similarity). FT METAL 450 450 Calcium (By similarity). FT VAR_SEQ 612 625 VLGPAMVGVAVTVE -> RAYPGASGEGLSPV (in FT isoform 2). FT /FTId=VSP_015103. FT VAR_SEQ 626 706 Missing (in isoform 2). FT /FTId=VSP_015104. FT VARIANT 58 58 M -> V (in dbSNP:rs2076405). FT /FTId=VAR_013250. SQ SEQUENCE 706 AA; 79312 MW; 97BBE2043C5FF834 CRC64; MAGIRVTKVD WQRSRNGAAH HTQEYPCPEL VVRRGQSFSL TLELSRALDC EEILIFTMET GPRASEALHT KAVFQTSELE RGEGWTAARE AQMEKTLTVS LASPPSAVIG RYLLSIRLSS HRKHSNRRLG EFVLLFNPWC AEDDVFLASE EERQEYVLSD SGIIFRGVEK HIRAQGWNYG QFEEDILNIC LSILDRSPGH QNNPATDVSC RHNPIYVTRV ISAMVNSNND RGVVQGQWQG KYGGGTSPLH WRGSVAILQK WLKGRYKPVK YGQCWVFAGV LCTVLRCLGI ATRVVSNFNS AHDTDQNLSV DKYVDSFGRT LEDLTEDSMW NFHVWNESWF ARQDLGPSYN GWQVLDATPQ EESEGVFRCG PASVTAIREG DVHLAHDGPF VFAEVNADYI TWLWHEDESR ERVYSNTKKI GRCISTKAVG SDSRVDITDL YKYPEGSRKE RQVYSKAVNR LFGVEASGRR IWIRRAGGRC LWRDDLLEPA TKPSIAGKFK VLEPPMLGHD LRLALCLANL TSRAQRVRVN LSGATILYTR KPVAEILHES HAVRLGPQEE KRIPITISYS KYKEDLTEDK KILLAAMCLV TKGEKLLVEK DITLEDFITI KVLGPAMVGV AVTVEVTVVN PLIERVKDCA LMVEGSGLLQ EQLSIDVPTL EPQERASVQF DITPSKSGPR QLQVDLVSPH FPDIKGFVIV HVATAK //