ID L8IUK1_9CETA Unreviewed; 732 AA. AC L8IUK1; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 24-JAN-2024, entry version 48. DE SubName: Full=Coagulation factor XIII A chain {ECO:0000313|EMBL:ELR59683.1}; GN ORFNames=E5288_WYG014887 {ECO:0000313|EMBL:MXQ96899.1}, M91_12590 GN {ECO:0000313|EMBL:ELR59683.1}; OS Bos mutus (wild yak). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR59683.1, ECO:0000313|Proteomes:UP000011080}; RN [1] {ECO:0000313|EMBL:ELR59683.1, ECO:0000313|Proteomes:UP000011080} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YakQH1 {ECO:0000313|EMBL:ELR59683.1}, and yakQH1 RC {ECO:0000313|Proteomes:UP000011080}; RX PubMed=22751099; DOI=10.1038/ng.2343; RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J., RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y., RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y., RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T., RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R., RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P., RA Wang J., Liu J.; RT "The yak genome and adaptation to life at high altitude."; RL Nat. Genet. 44:946-949(2012). RN [2] {ECO:0000313|EMBL:MXQ96899.1, ECO:0000313|Proteomes:UP000322234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WY2019 {ECO:0000313|EMBL:MXQ96899.1}; RC TISSUE=Blood {ECO:0000313|EMBL:MXQ96899.1}; RA Liu Y.; RT "The sequence and de novo assembly of the wild yak genome."; RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases. 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 EMBL; JH880690; ELR59683.1; -; Genomic_DNA. DR EMBL; VBQZ03000176; MXQ96899.1; -; Genomic_DNA. DR RefSeq; XP_005891215.1; XM_005891153.2. DR AlphaFoldDB; L8IUK1; -. DR STRING; 72004.ENSBMUP00000026582; -. DR Ensembl; ENSBMUT00000030610; ENSBMUP00000026582; ENSBMUG00000019970. DR GeneID; 102282528; -. DR KEGG; bom:102282528; -. DR CTD; 2162; -. DR OrthoDB; 5344745at2759; -. DR Proteomes; UP000011080; Unassembled WGS sequence. DR Proteomes; UP000322234; 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 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:SF42; COAGULATION FACTOR XIII A CHAIN; 1. DR PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 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; 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:UP000011080}. FT DOMAIN 307..400 FT /note="Transglutaminase-like" FT /evidence="ECO:0000259|SMART:SM00460" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 315 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 374 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT ACT_SITE 397 FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1" FT BINDING 437 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 439 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 486 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" FT BINDING 491 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2" SQ SEQUENCE 732 AA; 82731 MW; C6BBE8B7D374D697 CRC64; MSESSGTAFG GRRAIPPNTS NAAENDPPTV ELQGLVPRGF NPQDYLNVTN VHLFKERWDS NKVDHHTDKY SNDKLIVRRG QSFYIQIDFN RPYDPRRDLF RVEYVIGLYP QENKGTYIPV PLVSELQSGK WGAKVVMRED RSVRLSVQSS ADCIVGKFRM YVAVWTPYGV IRTSRNPETD TYILFNPWCE EDAVYLENEK EREECVLNDI GVIFYGDFND IKSRSWSYGQ FEDSILDACL FVMDKANMDL SGRGNPIKVS RVGSAMINAK DDEGVIAGSW DNVYAYGVPP SAWTGSVDIL LEYKSSQKPV RYGQCWVFAG VFNTFLRCLG IPARVVTNYF SAHDNDANLQ LDIFLEEDGN VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQVVDSTP QENSDGMYRC GPASVQAIKH GHVCFQFDAP FVFAEVNSDL VYVTAKKDGT HVVEALDTTH IGKLIVTKEI GGDGMKDITD TYKFQEGQEE ERLALETAMM YGAKKALNTE GVLKSKSDVR MNFEVENAVL GRDLKVIITF RNNGSARYTV TAYLSGNISF YTGVSKAEFK NETFEVTLEP LSFKREEVLI GAGEYMGQLL EQAFLHFFVT ARVNETRDVL AKQKSIALTV PKVVIKVRGA QVVGSDMVVT VEFTNPLKET LRNVWIRLDG PGVTKPLRKM FREIRPNSTV QWEELCRPWV SGPRKLIASL TSDSLRHVYG ELDLQIQRRP SM //