CAD22_RAT
ID CAD22_RAT Reviewed; 813 AA.
AC Q63315; Q63561;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cadherin-22;
DE AltName: Full=Pituitary and brain cadherin;
DE Short=PB-cadherin;
DE Flags: Precursor;
GN Name=Cdh22;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND CHARACTERIZATION.
RC STRAIN=Wistar; TISSUE=Brain, and Pituitary;
RX PubMed=8626716; DOI=10.1074/jbc.271.19.11548;
RA Sugimoto K., Honda S., Yamamoto T., Ueki T., Monden M., Kaji A.,
RA Matsumoto K., Nakamura T.;
RT "Molecular cloning and characterization of a newly identified member of the
RT cadherin family, PB-cadherin.";
RL J. Biol. Chem. 271:11548-11556(1996).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q63315-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63315-2; Sequence=VSP_000643, VSP_000644;
CC -!- TISSUE SPECIFICITY: Strongly expressed in the pituitary gland and the
CC brain (in the inner granular and glomerular layers of the olfactory
CC bulb, anterior olfactory nucleus, primary olfactory cortex, Purkinje
CC cell layer of cerebellum, and pineal gland). Low expression in lung and
CC heart. No expression in submandibular gland, thymus, liver, spleen,
CC adrenal, and kidney.
CC -!- DEVELOPMENTAL STAGE: Expressed strongly in fetal brain.
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; D83348; BAA11894.1; -; mRNA.
DR EMBL; D83349; BAA11895.1; -; mRNA.
DR RefSeq; NP_062034.2; NM_019161.2. [Q63315-1]
DR AlphaFoldDB; Q63315; -.
DR SMR; Q63315; -.
DR STRING; 10116.ENSRNOP00000025150; -.
DR GlyGen; Q63315; 3 sites.
DR PaxDb; Q63315; -.
DR PRIDE; Q63315; -.
DR Ensembl; ENSRNOT00000025150; ENSRNOP00000025150; ENSRNOG00000018557. [Q63315-1]
DR GeneID; 29182; -.
DR KEGG; rno:29182; -.
DR UCSC; RGD:2321; rat. [Q63315-1]
DR CTD; 64405; -.
DR RGD; 2321; Cdh22.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000159376; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q63315; -.
DR OMA; KHTGIIM; -.
DR OrthoDB; 242083at2759; -.
DR PhylomeDB; Q63315; -.
DR PRO; PR:Q63315; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000018557; Expressed in frontal cortex and 7 other tissues.
DR Genevisible; Q63315; RN.
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; IEP:RGD.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:RGD.
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 Alternative splicing; 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_0000003823"
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 VAR_SEQ 668..694
FT /note="NDEGGGEQDTEAYDMSALRSLYDFGEL -> TLGSGHRGTSNKEDHQCPASL
FT SLGFKP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8626716"
FT /id="VSP_000643"
FT VAR_SEQ 695..813
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8626716"
FT /id="VSP_000644"
SQ SEQUENCE 813 AA; 87979 MW; 30BEA60B5D2D467B CRC64;
MRPRPAGALR AGAALSPVLL LLLLLQLLGH LWAASTPAPS SLSPGTQQDN 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 FYFRLVPEEP
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
