CAD22_MOUSE
ID CAD22_MOUSE Reviewed; 813 AA.
AC Q9WTP5; I7HIP9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cadherin-22;
DE AltName: Full=Pituitary and brain cadherin;
DE Short=PB-cadherin;
DE Flags: Precursor;
GN Name=Cdh22;
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=10398531;
RX DOI=10.1002/(sici)1097-0177(199907)215:3<206::aid-aja3>3.0.co;2-x;
RA Kitajima K., Koshimizu U., Nakamura T.;
RT "Expression of a novel type of classic cadherin, PB-cadherin in developing
RT brain and limb buds.";
RL Dev. Dyn. 215:206-214(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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. PB-cadherins may have a role in the
CC morphological organization of pituitary gland and brain tissues.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Abundant in
CC olfactory bulb, cerebrum, and cerebellum, less in pons, medulla, and
CC spinal cord. Low expression in heart. No expression in lung, liver,
CC spleen, kidney, testis, stomach, intestine, colon, and placenta.
CC -!- DEVELOPMENTAL STAGE: Expressed at 9.5 dpc onwards. At 10.5 dpc, in
CC brain (telencephalic vesicles and isthmus), spinal cord and limb buds
CC (in the zone of polarizing activity). At 14.5 dpc, in olfactory bulb
CC and cerebellum. {ECO:0000269|PubMed:10398531}.
CC -!- INDUCTION: Down-regulated by thyroid hormone.
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}.
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; AB019618; BAA34426.1; -; mRNA.
DR EMBL; AL591411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17073.1; -.
DR RefSeq; NP_778153.2; NM_174988.3.
DR PDB; 6CG7; X-ray; 2.71 A; A/B=60-266.
DR PDBsum; 6CG7; -.
DR AlphaFoldDB; Q9WTP5; -.
DR SMR; Q9WTP5; -.
DR STRING; 10090.ENSMUSP00000066864; -.
DR GlyGen; Q9WTP5; 3 sites.
DR iPTMnet; Q9WTP5; -.
DR PhosphoSitePlus; Q9WTP5; -.
DR PaxDb; Q9WTP5; -.
DR PRIDE; Q9WTP5; -.
DR ProteomicsDB; 281743; -.
DR Antibodypedia; 2513; 125 antibodies from 22 providers.
DR DNASU; 104010; -.
DR Ensembl; ENSMUST00000065438; ENSMUSP00000066864; ENSMUSG00000053166.
DR GeneID; 104010; -.
DR KEGG; mmu:104010; -.
DR UCSC; uc008nxc.2; mouse.
DR CTD; 64405; -.
DR MGI; MGI:1341843; Cdh22.
DR VEuPathDB; HostDB:ENSMUSG00000053166; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000159376; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q9WTP5; -.
DR OMA; KHTGIIM; -.
DR OrthoDB; 242083at2759; -.
DR PhylomeDB; Q9WTP5; -.
DR TreeFam; TF329887; -.
DR BioGRID-ORCS; 104010; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9WTP5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9WTP5; protein.
DR Bgee; ENSMUSG00000053166; Expressed in motor neuron and 142 other tissues.
DR ExpressionAtlas; Q9WTP5; baseline and differential.
DR Genevisible; Q9WTP5; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
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; 5.
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; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..813
FT /note="Cadherin-22"
FT /id="PRO_0000003822"
FT TOPO_DOM 34..621
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..813
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 61..165
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 166..274
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 275..391
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 392..495
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 496..613
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 696..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 199
FT /note="S -> R (in Ref. 1; BAA34426)"
FT /evidence="ECO:0000305"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:6CG7"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6CG7"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:6CG7"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 128..138
FT /evidence="ECO:0007829|PDB:6CG7"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 144..156
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6CG7"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:6CG7"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:6CG7"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:6CG7"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6CG7"
FT STRAND 255..265
FT /evidence="ECO:0007829|PDB:6CG7"
SQ SEQUENCE 813 AA; 87953 MW; BC0267FD6A6B15D8 CRC64;
MRPRPEGALR AGAALSPVLL FLLLLPLLGH LWAASTPAPS SLSPGAQEDN QLGAGRVKRG
WVWNQFFVVE EYTGTEPLYV GKIHSDSDEG DGTIKYTISG EGAGTIFLID ELTGDIHATE
RLDREQKTFY TLRAQARDRA TNRLLEPESE FIIKVQDIND SEPRFLHGPY IGSVAELSPT
GTSVMQVMAS DADDPTYGSS ARLVYSVLDG EHHFTVDPKT GVIRTAVPDL DRESQERYEV
VIQATDMAGQ LGGLSGSTTV TIVVTDVNDN PPRFPQKMYQ FSIQESAPIG TAVGRVKAED
SDVGENTDMT YHLREESGSG GDAFKVTTDS DTQEAIIVVQ KHLDFESQQV HTVVLEALNK
FVDPRFADLG TFRDQAIVRV AVTDVDEPPE FRPPSGLLEV QEDAQVGSLV GVVTARDPDA
ANRPVRYAID RDSDLEQIFD IDADTGAIVT GKGLDRETAG WHNITVLAME ADNHAQLSRA
SLRIRILDVN DNPPELATPY EAAVCEDAKP GQLIQTISVV DRDEPQGGHR FYFRLVPEAP
SNPHFSLLDI EDNTAAVHTQ HVGFNRQEQD VFLLPILVVD SGPPTLSSTG TLTIRICGCD
SSGTIQSCNT TAFVMAASLS PGALIALLVC VLILVVLALL ILTLRRHHKS HLSSDVDEDM
RDNVIKYNDE GGGEQDTEAY DMSALRSLYD FGELKGGDPG GGAASPPQAA SSSERHSLPR
GPSSPEPDFS VFRDFISRKV ALADADLSVP PYDAFQTYAF EGAGSPAASL SSLHSGSTGS
EQDFAFLRAW GPRFRPLAAL YAGHRGDDEA PAS
