ID A0A1S3AKC9_ERIEU Unreviewed; 810 AA.
AC A0A1S3AKC9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase K {ECO:0000256|ARBA:ARBA00040559};
DE EC=2.3.2.13 {ECO:0000256|ARBA:ARBA00024222};
DE AltName: Full=Epidermal TGase {ECO:0000256|ARBA:ARBA00043229};
DE AltName: Full=Transglutaminase K {ECO:0000256|ARBA:ARBA00041726};
DE AltName: Full=Transglutaminase-1 {ECO:0000256|ARBA:ARBA00041651};
GN Name=TGM1 {ECO:0000313|RefSeq:XP_007536319.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007536319.1};
RN [1] {ECO:0000313|RefSeq:XP_007536319.1}
RP IDENTIFICATION.
RG RefSeq;
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 -!- SUBUNIT: Interacts with PLAAT4. {ECO:0000256|ARBA:ARBA00038573}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-
CC anchor {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC Transglutaminase family. {ECO:0000256|ARBA:ARBA00005968}.
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DR RefSeq; XP_007536319.1; XM_007536257.2.
DR AlphaFoldDB; A0A1S3AKC9; -.
DR STRING; 9365.ENSEEUP00000007593; -.
DR GeneID; 103125470; -.
DR CTD; 7051; -.
DR eggNOG; ENOG502QQ46; Eukaryota.
DR InParanoid; A0A1S3AKC9; -.
DR OrthoDB; 5344745at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
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:SF49; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE K; 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 Keratinization {ECO:0000256|ARBA:ARBA00023249};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000459-2};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT DOMAIN 363..456
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 371
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 430
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 453
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 493
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 495
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 810 AA; 89155 MW; 89F2051882B498A3 CRC64;
MDGSRSDVGR WGRSFWQPSG TPSPEPEPEP EPDRRSRRGG RSFWARCCGC CSCRNGPDED
WGSEPYGDRS SRGRGSSAGG RRPDSRSGGT VNAAGDGTIR DGMLVVTGVD LLSSRSDHNR
REHHTDEFEY DELIIRRGQP FHIVLFLSRP YESSDRIALE LLIGSNPEVG KGTHIIIPVG
KGGSGGWKAQ VTKSSGQNLN LRVHTSPNAI IGKFQFTVRT RSEAGEFQLP FDPHNEIYIL
FNPWCPDDIV YVGHEDWRQE YVLNESGRIY YGTEAQIGER TWNYGQFDHG VLDACLYILD
RRGMPYGGRG DPVSVSRVIS AMVNSLDDNG VLIGNWTGDY SRGTNPSAWV GSVEILLSYL
RTGSSVPYGQ CWVFAGVTTT VLRCLGLATR TVTNFNSAHD TDTSLTMDIY FDENMKPLEH
LNHDSVWNFH VWNDCWMKRP DLPSGFDGWQ VVDATPQETS SGIFCCGPCS VQSIKNGLVY
MKYDTPFIFA EVNSDKVYWQ RQDDGSFKIV YVEEKAIGTL IVTKAIGSNM QEEITSLYKH
PEGSEAERKA VETAAAHGSK PNVYATRDSA EDVAIQVEAQ DASVGQDLML SVVLTNRGSS
RRTVKLHLYL SVTYYTGVTG SVFKDSKKEV TLAPGASDRV EMPVAYREYK PHLVDQGAML
LNVSGHVKES GQVLAKQHTF RLRTPDLSLT LLGAAVVGQE CEVQIVFKNP LPTTLTNVVF
RLEGSGLQRP KILNVGDIGG NETVTLRQTF VPVRPGPRQL IASLDSPQLS QVHGVIQVDV
SPASGDRSFS TAGGDSREEE SIPMASRGGA
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