ID G1TTF3_RABIT Unreviewed; 613 AA.
AC G1TTF3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=ADAM metallopeptidase domain 18 {ECO:0008006|Google:ProtNLM};
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:ENSOCUP00000020323.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000020323.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {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:ENSOCUP00000020323.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000020323.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR AlphaFoldDB; G1TTF3; -.
DR SMR; G1TTF3; -.
DR PaxDb; 9986-ENSOCUP00000020323; -.
DR Ensembl; ENSOCUT00000025069.3; ENSOCUP00000020323.3; ENSOCUG00000023766.3.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000162466; -.
DR HOGENOM; CLU_012714_4_3_1; -.
DR InParanoid; G1TTF3; -.
DR TreeFam; TF314733; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000023766; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905:SF26; A DISINTEGRIN AND METALLOPEPTIDASE DOMAIN 3; 1.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 93..277
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 287..376
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT DOMAIN 510..544
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 233..238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 348..368
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
FT DISULFID 534..543
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 613 AA; 68436 MW; 74E948EB75C0F5ED CRC64;
MYCFYQGYSK EFPKSAVTLS ICSGLRGLLQ FENVSYGIEP LDSSANNEHI VFQTKNNKIG
YPLFQKNHLT NQYVSSSYRI LVKSEKQTFA FQYDVMGSEE ELVAEKVIRI FSLINSMFSQ
FKITVMLSTL ELWSDKNKIS TNGDAEEILK RFLSWKQNDP FQNPHEMSYL FIYRDYATFV
GTTYHGMACD PKFATGVALY PNMGTLEAFS VVVVQLLGIN LGLTYDDIYN CYCPGPMCIM
NPEAILSSGI KFFSSCSMEE FKQSVSLPKF ECLQYKEVPT VVFQGKSGTC GNGILEGSEQ
CDCGVGESCS HKKCCNPVDC TLIGFSECGT GPCCDAKTCL IANRGKLCRK STDPCDFPEF
CNGTSEFCVP DVKSADLEPC NNKTAFCFKG RCRDRDRQCL GIFGEFAKSG TYLCEEELNF
HNDKFGSCRR QCNYNFVLCG KLACRWTKAV LAPSKEYDVQ YTYINDQICV TASLRNVSRS
DDTFVEHGSV CGEKKICLNG ECKILNAYAE KPNCDSQTLC QGHGVCNERL NCHCDAGYSP
PRCDETAFSP GGSVDDGFWL PTSKSHGAAQ SSCSAEQFQI SALGVKELKA RRLRIKDISR
RLLECFSLPP QIP
//
