CAD11_MOUSE
ID CAD11_MOUSE Reviewed; 796 AA.
AC P55288;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cadherin-11;
DE AltName: Full=OSF-4;
DE AltName: Full=Osteoblast cadherin;
DE Short=OB-cadherin;
DE Flags: Precursor;
GN Name=Cdh11; Synonyms=Cad-11;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7750649; DOI=10.1006/dbio.1995.1148;
RA Hoffmann I.H., Balling R.;
RT "Cloning and expression analysis of a novel mesodermally expressed
RT cadherin.";
RL Dev. Biol. 169:337-346(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7750650; DOI=10.1006/dbio.1995.1149;
RA Kimura Y., Matsunami H., Inoue T., Shimamura K., Uchida N., Ueno T.,
RA Miyazaki T., Takeichi M.;
RT "Cadherin-11 expressed in association with mesenchymal morphogenesis in the
RT head, somite, and limb bud of early mouse embryos.";
RL Dev. Biol. 169:347-358(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Calvaria;
RX PubMed=8163513; DOI=10.1016/s0021-9258(17)32685-6;
RA Okazaki M., Takeshita S., Kawai S., Kikuno R., Tsujimura A., Kudo A.,
RA Amann E.;
RT "Molecular cloning and characterization of OB-cadherin, a new member of
RT cadherin family expressed in osteoblasts.";
RL J. Biol. Chem. 269:12092-12098(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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 [5]
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=8879495; DOI=10.1095/biolreprod55.4.822;
RA Munro S.B., Blaschuk O.W.;
RT "A comprehensive survey of the cadherins expressed in the testes of fetal,
RT immature, and adult mice utilizing the polymerase chain reaction.";
RL Biol. Reprod. 55:822-827(1996).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND THR-791, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types.
CC -!- SUBUNIT: Interacts with PCDH8. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Selectively expressed in osteoblastic cell lines,
CC precursor cell lines of osteoblasts, and primary osteoblastic cells
CC from calvaria, as well as in lung, testis, and brain tissues at low
CC levels.
CC -!- DEVELOPMENTAL STAGE: In the testis, expression is highest in fetal
CC gonad and decreases 8-fold in newborn. {ECO:0000269|PubMed:8879495}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
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DR EMBL; X77557; CAA54674.1; -; mRNA.
DR EMBL; D31963; BAA06730.1; -; mRNA.
DR EMBL; D21253; BAA04797.1; -; mRNA.
DR EMBL; BC046314; AAH46314.1; -; mRNA.
DR CCDS; CCDS22571.1; -.
DR PIR; A53584; A53584.
DR PIR; I48277; I48277.
DR PIR; I49556; I49556.
DR RefSeq; NP_033996.4; NM_009866.5.
DR RefSeq; XP_006530686.1; XM_006530623.3.
DR RefSeq; XP_006530687.1; XM_006530624.2.
DR RefSeq; XP_006530689.1; XM_006530626.3.
DR PDB; 2A4C; X-ray; 2.90 A; A/B=54-151.
DR PDB; 2A4E; X-ray; 3.20 A; A=54-260.
DR PDB; 6CGB; X-ray; 2.99 A; A=54-155.
DR PDBsum; 2A4C; -.
DR PDBsum; 2A4E; -.
DR PDBsum; 6CGB; -.
DR AlphaFoldDB; P55288; -.
DR SMR; P55288; -.
DR BioGRID; 198632; 4.
DR DIP; DIP-59088N; -.
DR IntAct; P55288; 3.
DR MINT; P55288; -.
DR STRING; 10090.ENSMUSP00000074681; -.
DR ChEMBL; CHEMBL2163173; -.
DR GlyConnect; 2164; 5 N-Linked glycans (1 site).
DR GlyGen; P55288; 2 sites, 5 N-linked glycans (1 site).
DR iPTMnet; P55288; -.
DR PhosphoSitePlus; P55288; -.
DR jPOST; P55288; -.
DR MaxQB; P55288; -.
DR PaxDb; P55288; -.
DR PeptideAtlas; P55288; -.
DR PRIDE; P55288; -.
DR ProteomicsDB; 265493; -.
DR Antibodypedia; 4584; 822 antibodies from 38 providers.
DR DNASU; 12552; -.
DR Ensembl; ENSMUST00000075190; ENSMUSP00000074681; ENSMUSG00000031673.
DR GeneID; 12552; -.
DR KEGG; mmu:12552; -.
DR UCSC; uc009mzu.1; mouse.
DR CTD; 1009; -.
DR MGI; MGI:99217; Cdh11.
DR VEuPathDB; HostDB:ENSMUSG00000031673; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000153691; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; P55288; -.
DR OMA; ERYFVIN; -.
DR OrthoDB; 188978at2759; -.
DR PhylomeDB; P55288; -.
DR TreeFam; TF329887; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 12552; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Cdh11; mouse.
DR EvolutionaryTrace; P55288; -.
DR PRO; PR:P55288; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P55288; protein.
DR Bgee; ENSMUSG00000031673; Expressed in vault of skull and 288 other tissues.
DR Genevisible; P55288; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0021957; P:corticospinal tract morphogenesis; IGI:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..53
FT /evidence="ECO:0000255"
FT /id="PRO_0000003787"
FT CHAIN 54..796
FT /note="Cadherin-11"
FT /id="PRO_0000003788"
FT TOPO_DOM 54..617
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 641..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..159
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 160..268
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 269..383
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 384..486
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 487..612
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 791
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 462
FT /note="E -> D (in Ref. 1; CAA54674)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="T -> L (in Ref. 2; BAA06730)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="D -> N (in Ref. 2; BAA06730)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="V -> M (in Ref. 1; CAA54674)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="P -> Q (in Ref. 2; BAA06730)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="L -> P (in Ref. 2; BAA06730)"
FT /evidence="ECO:0000305"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2A4C"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:2A4C"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2A4C"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2A4C"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:2A4C"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:2A4C"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:2A4E"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:2A4E"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2A4E"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2A4E"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:2A4E"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:2A4E"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:2A4E"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2A4E"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2A4E"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2A4E"
FT STRAND 230..239
FT /evidence="ECO:0007829|PDB:2A4E"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:2A4E"
FT STRAND 249..259
FT /evidence="ECO:0007829|PDB:2A4E"
SQ SEQUENCE 796 AA; 88112 MW; 0D584D24641DD529 CRC64;
MKENYCLQAA LVCLSMLYHS QAFALERRSH LHPSFHGHHE KGKEGQVLQR SKRGWVWNQF
FVIEEYTGPD PVLVGRLHSD IDSGDGNIKY ILSGEGAGTI FVIDDKSGNI HATKTLDREE
RAQYTLMAQA VDRDTNRPLE PPSEFIVKVQ DINDNPPEFL HEIYHANVPE RSNVGTSVIQ
VTASDADDPT YGNSAKLVYS ILEGQPYFSV EAQTGIIRTA LPNMDREAKE EYHVVIQAKD
MGGHMGGLSG TTKVTITLTD VNDNPPKFPQ SVYQMSVSEA AVPGEEVGRV KAKDPDIGEN
GLVTYNIVDG DGIELFEITT DYETQDGVVK LKKPVDFETK RAYSLKIEAA NVHIDPKFIS
NGPFKDTVTV KISVEDADEP PMFLAPSYIH EVQENAAAGT VVGRVHAKDP DAANSPIRYS
IDRHTDLDRF FTINPEDGFI KTTKPLDREE TAWLNISVFA AEIHNRHQET KVPVAIRVLD
VNDNAPKFAA PYEGFICESD HPKALSNQPI VTVSADDQDD TANGPRFIFS LPPEIMHNPN
FTVRDNRDNT AGVYARRGGF SRQKQDFYLL PIVISDGGIP PMSSTNTLTI KVCGCDVNGA
LLSCNAEAYI LNAGLSTGAL IAILACIVIL LVIVVLFVTL RRQKKEPLIV FEEEDVRENI
ITYDDEGGGE EDTEAFDIAT LQNPDGINGF IPRKDIKPEY QYMPRPGLRP APNSVDVDDF
INTRIQEADN DPTAPPYDSI QIYGYEGRGS VAGSLSSLES ATTDSDLDYD YLQNWGPRFK
KLADLYGSKD TFDDDS
