ID C4P259_STRPU Unreviewed; 751 AA.
AC C4P259;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Nuclear transglutaminase {ECO:0000313|EMBL:ACQ66512.1};
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668 {ECO:0000313|EMBL:ACQ66512.1};
RN [1] {ECO:0000313|EMBL:ACQ66512.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19403662; DOI=10.1242/dev.030775;
RA Wong J.L., Wessel G.M.;
RT "Extracellular matrix modifications at fertilization: regulation of
RT dityrosine crosslinking by transamidation.";
RL Development 0:0-0(2009).
RN [2] {ECO:0000313|Proteomes:UP000007110}
RP NUCLEOTIDE SEQUENCE.
RA Murali S., Liu Y., Vee V., English A., Wang M., Skinner E., Han Y.,
RA Muzny D.M., Worley K.C., Gibbs R.A.;
RT "Genome sequencing for Strongylocentrotus purpuratus.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:NP_001154911}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JAN-2021) 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}.
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DR EMBL; FJ829471; ACQ66512.1; -; mRNA.
DR RefSeq; NP_001154911.1; NM_001161439.1.
DR AlphaFoldDB; C4P259; -.
DR STRING; 7668.C4P259; -.
DR EnsemblMetazoa; NM_001161439; NP_001154911; LOC592303.
DR GeneID; 592303; -.
DR KEGG; spu:592303; -.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR HOGENOM; CLU_326622_0_0_1; -.
DR InParanoid; C4P259; -.
DR OMA; REREICQ; -.
DR OrthoDB; 5344745at2759; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IBA:GO_Central.
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:SF40; HEMOCYTE PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE-LIKE PROTEIN; 1.
DR PANTHER; PTHR11590; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 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 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:UP000007110}.
FT DOMAIN 321..415
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 329
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 389
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 412
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 751 AA; 83918 MW; 42074B51E03F7EE0 CRC64;
MSTLMETADE TGAGITSPPS PGRSVNVADA ERAYLGEGRD DDTDSPSNPN QLSVKNFDYE
LVRNRERHHT SEYEIKNLFV RRGQAFDLDV TFNKVPKTEV FMLELTVRGA VVSSINRGTV
IRMPFHRSQA DTPGGWGIRV GSTEGAKYSL VINCPSDAIV SRYNVAVVIK DTEEAEPRYF
RQDDPIYVLF NAWCREDSVH MAGDIEKGEY VLNDNGYVFI GSARPGSQHP RPWVFGQFED
SATEVVFDLL EKWVRVNARS DPVVVSRKFT HLINYMPEYG VPETKVGLLV GNWSGDYEGG
ESPSKWTGST KIYETFAESG GKPVNYGQCW VFSGVLCTAM RCLGIPCRSV TNFASAHDTD
VSMTIDTVID SETNEEIEYL SNDSVWNFHV WNEVYYSRSD TIPGMGGWQV VDATPQESSE
GVFQCGPAPV TAIKQGLTYI NYDTKFAFAE VNADRINWVA TKKDRGPPDM KTVSINTNAV
GKYISTKKLP LVPGGYISRW NARNDITLEY KYAEGSVEER NAVERAISYG TRPNTYREDV
KTDDIEMAIV LDEKISVGSD FELKVAVNNK SSVSRVISLT MNAHMCYYTG VLAKKITSLR
KELTVPAGKS EHVIEMIRAE IYSSCLVDQA CIKFYVYGKV KETSQQTVSQ DTVYLTPPEM
KTEFKVVGHE VEAVVEFVNP LPITLTNCTI TFEGARLLRS MTLYANDVPS KGNFKQKVKF
SPREKGKRTL VIDFDSKQIG NITDVVEIEI P
//