ID G1SES6_RABIT Unreviewed; 741 AA.
AC G1SES6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Transglutaminase 3 {ECO:0000313|Ensembl:ENSOCUP00000000969.3};
GN Name=TGM3 {ECO:0000313|Ensembl:ENSOCUP00000000969.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000000969.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000000969.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000000969.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000000969.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000000969.3};
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}.
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DR EMBL; AAGW02060584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02060585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02060586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02060587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02060588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02060589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SES6; -.
DR SMR; G1SES6; -.
DR STRING; 9986.ENSOCUP00000000969; -.
DR PaxDb; 9986-ENSOCUP00000000969; -.
DR Ensembl; ENSOCUT00000001116.4; ENSOCUP00000000969.3; ENSOCUG00000001114.4.
DR eggNOG; ENOG502QUPB; Eukaryota.
DR GeneTree; ENSGT01050000244866; -.
DR HOGENOM; CLU_013435_1_0_1; -.
DR InParanoid; G1SES6; -.
DR OMA; SMVGWNF; -.
DR TreeFam; TF324278; -.
DR Proteomes; UP000001811; Chromosome 4.
DR Bgee; ENSOCUG00000001114; Expressed in skin of back and 8 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; 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; 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:SF36; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE E; 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.
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:UP000001811}.
FT DOMAIN 313..405
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 321
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 379
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT ACT_SITE 402
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-1"
FT BINDING 442
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 444
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
FT BINDING 497
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR000459-2"
SQ SEQUENCE 741 AA; 82092 MW; 359A27A63C2B0CFB CRC64;
MAPGAEKSQD LDSRPPLPPW RKAEMPLGGE KCVHQPGENT TGNHQITAGA LEPQSINWQM
TSNRRAHHTD KFSGQNLILR RGQPFDMLLA LNRPLGSGES LEFTVSTGPY PSESTGTKAV
FPLSSGTGRG GWSAVLKGSS DNILTITLSS PASAPIGWYT LNMQISSQGT VSSLKLGTFI
LLFNPWLQAD DVFLSNHAER QEYVEEDAGI IYVGSTNRIG MVGWNFGQFE EDILNICLSI
LDKSLNFRRD PATDVALRKD PKYVGRVLSA MINSNDDNGV IAGNWSGNYA GGRDPRNWNG
SVEILKEWKK SGYKPVRFGQ CWVFAGALNT VLRCLGIPSR VITNFNSAHD TNRNLSVDVY
YDPMGNPLDR GSDSVWNFHV WNEGWFVRTD LGTQYDGWQV LDATPQEKSQ GVFQCGPSSV
HAVRDGDVDL DFDMSFVFAE VNADRITWIY DTASNSQKQN SLDTRSIGKY ISTKAVGSNS
RVDITDKYKY PEGSSEERRV FQKALGKLKP NAAFSPTSAR DLVEEERSPS ISGRFKITGV
LAVGKEVSLA LLLKNLTREK KTVTVNMTAW TIVYNGTLVH EVWKDSFTVD LDPEAETQHP
VTISYAQYDK YLKSDNMIRT TAICKVPKEA EVVVARDIIL DNPTLTLEVL DQAQVQKPVN
VQMLFSNPLD EPVKDCVLMV EGSGLLRGNL KIEVPALRPK ERSRVRFEIL PTRSGTKQLL
ADFSCNKFPA IKAMLSIDVA E
//
