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   04-NOV-2026, entry version 160.
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}.
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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   RefSeq; XP_036013049.1; XM_036157156.1.
DR   PDB; 6CG7; X-ray; 2.71 A; A/B=60-266.
DR   AlphaFoldDB; Q9WTP5; -.
DR   SMR; Q9WTP5; -.
DR   FunCoup; Q9WTP5; 36.
DR   STRING; 10090.ENSMUSP00000066864; -.
DR   GlyCosmos; Q9WTP5; 3 sites, No reported glycans.
DR   GlyGen; Q9WTP5; 3 sites, 2 N-linked glycans (2 sites).
DR   iPTMnet; Q9WTP5; -.
DR   PhosphoSitePlus; Q9WTP5; -.
DR   PaxDb; 10090-ENSMUSP00000066864; -.
DR   ProteomicsDB; 281743; -.
DR   Antibodypedia; 2513; 137 antibodies from 24 providers.
DR   DNASU; 104010; -.
DR   Ensembl; ENSMPUT00000017750; ENSMPUP00000017491; ENSMPUG00000017604.
DR   Ensembl; ENSMUST00000065438.13; ENSMUSP00000066864.7; ENSMUSG00000053166.15.
DR   GeneID; 104010; -.
DR   KEGG; mmu:104010; -.
DR   UCSC; uc008nxc.2; mouse.
DR   AGR; MGI:1341843; -.
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; ACEWKQQ; -.
DR   OrthoDB; 6252479at2759; -.
DR   PhylomeDB; Q9WTP5; -.
DR   BioGRID-ORCS; 104010; 1 hit in 78 CRISPR screens.
DR   PRO; PR:Q9WTP5; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9WTP5; protein.
DR   Bgee; ENSMUSG00000053166; Expressed in motor neuron and 143 other cell types or tissues.
DR   ExpressionAtlas; Q9WTP5; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:UniProtKB-ARBA.
DR   GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion; ISO:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell-cell adhesion; IEA:InterPro.
DR   CDD; cd11304; Cadherin_repeat; 5.
DR   FunFam; 4.10.900.10:FF:000007; Cadherin 22; 1.
DR   FunFam; 2.60.40.60:FF:000008; Cadherin 24; 1.
DR   FunFam; 2.60.40.60:FF:000009; Cadherin 24; 1.
DR   FunFam; 2.60.40.60:FF:000012; Cadherin 24; 1.
DR   FunFam; 2.60.40.60:FF:000017; Cadherin 24; 1.
DR   FunFam; 2.60.40.60:FF:000014; Cadherin 8; 1.
DR   Gene3D; 2.60.40.60; Cadherins; 5.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 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_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027:SF311; CADHERIN-22; 1.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin-like; 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
//