ID H2QS92_PANTR Unreviewed; 732 AA. AC H2QS92; A0A2J8MTU6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 27-MAR-2024, entry version 67. DE SubName: Full=Coagulation factor XIII A chain {ECO:0000313|Ensembl:ENSPTRP00000030210.3}; DE SubName: Full=Coagulation factor XIII, A1 polypeptide {ECO:0000313|EMBL:JAA39992.1}; GN Name=F13A1 {ECO:0000313|EMBL:JAA39992.1, GN ECO:0000313|Ensembl:ENSPTRP00000030210.3, ECO:0000313|VGNC:VGNC:7888}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000030210.3, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000030210.3, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the human RT genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|EMBL:JAA39992.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAA39992.1}; RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.; RT "De novo assembly of the reference chimpanzee transcriptome from NextGen RT mRNA sequences."; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPTRP00000030210.3} 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 EMBL; AACZ04065943; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ04065944; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ04065945; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ04065946; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ04065947; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ04065948; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AACZ04065949; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; GABE01004747; JAA39992.1; -; mRNA. DR RefSeq; XP_009448724.1; XM_009450449.2. DR STRING; 9598.ENSPTRP00000065448; -. DR Ensembl; ENSPTRT00000032699.4; ENSPTRP00000030210.3; ENSPTRG00000017694.6. DR GeneID; 462413; -. DR KEGG; ptr:462413; -. DR CTD; 2162; -. DR VGNC; VGNC:7888; F13A1. DR eggNOG; ENOG502QQ46; Eukaryota. DR GeneTree; ENSGT01050000244939; -. DR HOGENOM; CLU_013435_0_2_1; -. DR OMA; EEVCQPW; -. DR OrthoDB; 5344745at2759; -. DR TreeFam; TF324278; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000017694; Expressed in bone marrow and 16 other cell types or tissues. 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: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 2: Evidence at transcript level; KW Calcium {ECO:0000256|PIRSR:PIRSR000459-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}. FT DOMAIN 307..400 FT /note="Transglutaminase-like" FT /evidence="ECO:0000259|SMART:SM00460" FT REGION 1..27 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; 83291 MW; B2CBF4AFF850A54A CRC64; MSETSRTAFG GRRAVPPNNS NAAEDDLPTV ELQGVVPRGV NLQEFLNVTS VHLFKERWDT NKVDHHTDKY ENNKLIVRRG QSFYVQIDFN RPYDPRRDLF RVEYVIGRYP QENKGTYIPV PIVSELQSGK WGAKIVMRED RSVRLSIQSS PKCIVGKFRM YVAVWTPYGV LRTSRNPETD TYILFNPWCE DDAVYLDNEK EREEYVLNDI GVIFYGEVND IKTRSWSYGQ FEDGILDTCL YVMDRAQMDL SGRGNPIKVS RVGSAMVNAK DDEGVLVGSW DNIYAYGVPP SAWTGSVDIL LEYRSSENPV RYGQCWVFAG VFNTFLRCLG IPARIVTNYF SAHDNDANLQ MDIFLEEDGN VNSKLTKDSV WNYHCWNEAW MTRPDLPVGF GGWQAVDSTP QENSDGMYRC GPASVQAIKH GHVCFQFDAP FVFAEVNSDL IYITAKKDGT HVVENVDATH IGKLIVTKQI GGDGMMDITD TYKFQEGQEE ERLALETALM YGAKKPLNTE GVVKSRSNVD MDFEVENAVL GKDFKLSITF RNNSHNRYTI TAYLSANITF YTGVPKAEFK KETFDVTLEP LSFKKEAVLI QAGEYMGQLL EQASLHFFVT ARINETRDVL AKQKSTVLTI PEIIIKVRGT QVVGSDMTVT VEFTNPLKET LRNVWIHLDG PGITRPMKKM FREIRPNSTV QWEEVCRPWV SGHRKLIASM SSDSLRHVYG ELDVQIQRRP SM //