ID Q569W9_MOUSE Unreviewed; 468 AA. AC Q569W9; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 115. DE SubName: Full=Igh protein {ECO:0000313|EMBL:AAH92271.1}; GN Name=Igh {ECO:0000313|EMBL:AAH92271.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH92271.1}; RN [1] {ECO:0007829|PDB:1NBZ} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 20-235, AND DISULFIDE BONDS. RX PubMed=12515535; DOI=10.1021/bi020589+; RA Li Y., Urrutia M., Smith-Gill S.J., Mariuzza R.A.; RT "Dissection of binding interactions in the complex between the anti- RT lysozyme antibody HyHEL-63 and its antigen."; RL Biochemistry 42:11-22(2003). RN [2] {ECO:0000313|EMBL:AAH92271.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II {ECO:0000313|EMBL:AAH92271.1}; RC TISSUE=Mammary tumor metastatized to lung. Tumor arose spontaneously RC {ECO:0000313|EMBL:AAH92271.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] {ECO:0007829|PDB:1RUQ, ECO:0007829|PDB:1RUR} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 26-235, AND DISULFIDE BONDS. RX PubMed=14982995; DOI=10.1073/pnas.0307311101; RA Zhu X., Wentworth P., Wentworth A.D., Eschenmoser A., Lerner R.A., RA Wilson I.A.; RT "Probing the antibody-catalyzed water-oxidation pathway at atomic RT resolution."; RL Proc. Natl. Acad. Sci. U.S.A. 101:2247-2252(2004). 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; BC092271; AAH92271.1; -; mRNA. DR PDB; 1NBZ; X-ray; 1.85 A; B=20-235. DR PDB; 1RUQ; X-ray; 1.86 A; H=20-237. DR PDB; 1RUR; X-ray; 1.50 A; H=20-237. DR PDBsum; 1NBZ; -. DR PDBsum; 1RUQ; -. DR PDBsum; 1RUR; -. DR AlphaFoldDB; Q569W9; -. DR SMR; Q569W9; -. DR PeptideAtlas; Q569W9; -. DR ChiTaRS; Igh; mouse. DR EvolutionaryTrace; Q569W9; -. DR CDD; cd21817; IgC1_CH1_IgEG; 1. DR CDD; cd05768; IgC1_CH3_IgAGD_CH4_IgAEM; 1. DR CDD; cd04981; IgV_H; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 4. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR PANTHER; PTHR23411:SF28; IG GAMMA-2A CHAIN C REGION SECRETED FORM-RELATED; 1. DR PANTHER; PTHR23411; TAPASIN; 1. DR Pfam; PF07654; C1-set; 3. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00407; IGc1; 3. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; Immunoglobulin; 4. DR PROSITE; PS50835; IG_LIKE; 4. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1NBZ, ECO:0007829|PDB:1RUQ}; KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319}; KW Metal-binding {ECO:0007829|PDB:1RUQ, ECO:0007829|PDB:1RUR}; KW Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0007829|PDB:1RUQ, ECO:0007829|PDB:1RUR}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..468 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004251010" FT DOMAIN 19..137 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 144..236 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 259..358 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT DOMAIN 367..463 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT BINDING 189 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007829|PDB:1RUQ, ECO:0007829|PDB:1RUR" FT DISULFID 41..115 FT /evidence="ECO:0007829|PDB:1NBZ, ECO:0007829|PDB:1RUQ" FT DISULFID 165..220 FT /evidence="ECO:0007829|PDB:1NBZ, ECO:0007829|PDB:1RUQ" SQ SEQUENCE 468 AA; 51666 MW; 5BF6E527329F8461 CRC64; MEWSCIFLFL LSVTAGVHSE VQLQQSGAEL VRPGSSVKLS CKTSGYTFTS YYINWVKQRP GQGLEWIGHI YPGNGYTEYN EKFKGKATLT SDTSSSTAYM QLRSLTSENS AIYFCARTGG YDGYFDYWGQ GTTITVSSAK TTAPSVYPLA PVCGDTTGSS VTLGCLVKGY FPEPVTLTWN SGSLSSGVHT FPAVLQSDLY TLSSSVTVTS STWPSQSITC NVAHPASSTK VDKKIEPRGP TIKPCPPCKC PAPNLLGGPS VFIFPPKIKD VLMISLSPMV TCVVVDVSED DPDVQISWFV NNVEVLTAQT QTHREDYNST LRVVSALPIQ HQDWMSGKEF KCKVNNKALP APIERTISKP KGSVRAPQVY VLPPPEEEMT KKQVTLTCMV TDFMPEDIYV EWTNNGKTEL NYKNTEPVLD SDGSYFMYSK LRVEKKNWVE RNSYSCSVVH EGLHNHHTTK SFSRTPGK //