CAD22_HUMAN
ID CAD22_HUMAN Reviewed; 828 AA.
AC Q9UJ99; B9EGK7; O43205;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cadherin-22;
DE AltName: Full=Pituitary and brain cadherin;
DE Short=PB-cadherin;
DE Flags: Precursor;
GN Name=CDH22; Synonyms=C20orf25;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 449-828.
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; AL031687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75755.1; -; Genomic_DNA.
DR EMBL; BC136526; AAI36527.1; -; mRNA.
DR EMBL; AF035300; AAB88183.1; -; mRNA.
DR CCDS; CCDS13395.1; -.
DR RefSeq; NP_067071.1; NM_021248.2.
DR RefSeq; XP_011527296.1; XM_011528994.2.
DR AlphaFoldDB; Q9UJ99; -.
DR SMR; Q9UJ99; -.
DR BioGRID; 122159; 1.
DR STRING; 9606.ENSP00000437790; -.
DR GlyGen; Q9UJ99; 3 sites.
DR iPTMnet; Q9UJ99; -.
DR PhosphoSitePlus; Q9UJ99; -.
DR BioMuta; CDH22; -.
DR DMDM; 24211543; -.
DR MassIVE; Q9UJ99; -.
DR PaxDb; Q9UJ99; -.
DR PeptideAtlas; Q9UJ99; -.
DR PRIDE; Q9UJ99; -.
DR ProteomicsDB; 84607; -.
DR Antibodypedia; 2513; 125 antibodies from 22 providers.
DR DNASU; 64405; -.
DR Ensembl; ENST00000537909.4; ENSP00000437790.1; ENSG00000149654.11.
DR GeneID; 64405; -.
DR KEGG; hsa:64405; -.
DR MANE-Select; ENST00000537909.4; ENSP00000437790.1; NM_021248.3; NP_067071.1.
DR UCSC; uc010ghk.3; human.
DR CTD; 64405; -.
DR DisGeNET; 64405; -.
DR GeneCards; CDH22; -.
DR HGNC; HGNC:13251; CDH22.
DR HPA; ENSG00000149654; Tissue enriched (brain).
DR MIM; 609920; gene.
DR neXtProt; NX_Q9UJ99; -.
DR OpenTargets; ENSG00000149654; -.
DR PharmGKB; PA26295; -.
DR VEuPathDB; HostDB:ENSG00000149654; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000159376; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q9UJ99; -.
DR OMA; KHTGIIM; -.
DR OrthoDB; 242083at2759; -.
DR PhylomeDB; Q9UJ99; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; Q9UJ99; -.
DR SIGNOR; Q9UJ99; -.
DR BioGRID-ORCS; 64405; 12 hits in 1060 CRISPR screens.
DR ChiTaRS; CDH22; human.
DR GenomeRNAi; 64405; -.
DR Pharos; Q9UJ99; Tbio.
DR PRO; PR:Q9UJ99; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UJ99; protein.
DR Bgee; ENSG00000149654; Expressed in cerebellar vermis and 117 other tissues.
DR Genevisible; Q9UJ99; HS.
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; 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: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 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..828
FT /note="Cadherin-22"
FT /id="PRO_0000003821"
FT TOPO_DOM 36..624
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..828
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 64..168
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 169..277
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 278..394
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 395..498
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 499..616
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 702..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 828 AA; 89091 MW; 520F7B1D1F624DCA CRC64;
MRPRPEGRGL RAGVALSPAL LLLLLLPPPP TLLGRLWAAG TPSPSAPGAR QDGALGAGRV
KRGWVWNQFF VVEEYTGTEP LYVGKIHSDS DEGDGAIKYT ISGEGAGTIF LIDELTGDIH
AMERLDREQK TFYTLRAQAR DRATNRLLEP ESEFIIKVQD INDSEPRFLH GPYIGSVAEL
SPTGTSVMQV MASDADDPTY GSSARLVYSV LDGEHHFTVD PKTGVIRTAV PDLDRESQER
YEVVIQATDM AGQLGGLSGS TTVTIVVTDV NDNPPRFPQK MYQFSIQESA PIGTAVGRVK
AEDSDVGENT DMTYHLKDES SSGGDVFKVT TDSDTQEAII VVQKRLDFES QPVHTVILEA
LNKFVDPRFA DLGTFRDQAI VRVAVTDVDE PPEFRPPSGL LEVQEDAQVG SLVGVVTARD
PDAANRPVRY AIDRESDLDQ IFDIDADTGA IVTGKGLDRE TAGWHNITVL AMEADNHAQL
SRASLRIRIL DVNDNPPELA TPYEAAVCED AKPGQLIQTI SVVDRDEPQG GHRFYFRLVP
EAPSNPHFSL LDIQDNTAAV HTQHVGFNRQ EQDVFFLPIL VVDSGPPTLS STGTLTIRIC
GCDSSGTIQS CNTTAFVMAA SLSPGALIAL LVCVLILVVL VLLILTLRRH HKSHLSSDED
EDMRDNVIKY NDEGGGEQDT EAYDMSALRS LYDFGELKGG DGGGSAGGGA GGGSGGGAGS
PPQAHLPSER HSLPQGPPSP EPDFSVFRDF ISRKVALADG DLSVPPYDAF QTYAFEGADS
PAASLSSLHS GSSGSEQDFA YLSSWGPRFR PLAALYAGHR GDDEAQAS
