CADH9_MOUSE
ID CADH9_MOUSE Reviewed; 786 AA.
AC P70407;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Cadherin-9;
DE AltName: Full=T1-cadherin;
DE Flags: Precursor;
GN Name=Cdh9;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 679-786, AND 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 733-772.
RC STRAIN=CBA/J; TISSUE=Thymocyte;
RX PubMed=8620560; DOI=10.1006/cimm.1996.0123;
RA Munro S.B., Duclos A.J., Jackson A.R., Baines M.G., Blaschuk O.W.;
RT "Characterization of cadherins expressed by murine thymocytes.";
RL Cell. Immunol. 169:309-312(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.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Not detected in fetal, newborn or 7-day-old
CC testis. Present in 21-day-old and adult testes. Levels are 10-fold
CC higher in adult testis than in testis of 21-day-old animals.
CC {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; AC116724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U69136; AAB87707.1; -; mRNA.
DR AlphaFoldDB; P70407; -.
DR SMR; P70407; -.
DR STRING; 10090.ENSMUSP00000026432; -.
DR GlyConnect; 2173; 2 N-Linked glycans (2 sites).
DR GlyGen; P70407; 5 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; P70407; -.
DR PhosphoSitePlus; P70407; -.
DR PaxDb; P70407; -.
DR PRIDE; P70407; -.
DR ProteomicsDB; 281745; -.
DR MGI; MGI:107433; Cdh9.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; P70407; -.
DR PhylomeDB; P70407; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR ChiTaRS; Cdh9; mouse.
DR PRO; PR:P70407; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70407; protein.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0030424; C:axon; IDA:SynGO-UCL.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:SynGO-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO-UCL.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IPI:SynGO-UCL.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:SynGO-UCL.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0007416; P:synapse assembly; IDA:SynGO-UCL.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA: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; 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; Cleavage on pair of basic residues;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..52
FT /evidence="ECO:0000255"
FT /id="PRO_0000269661"
FT CHAIN 53..786
FT /note="Cadherin-9"
FT /id="PRO_0000126645"
FT TOPO_DOM 22..614
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..158
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 159..267
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 268..382
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 383..487
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 487..604
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97326"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 681
FT /note="A -> AK (in Ref. 2; AAB87707)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="M -> S (in Ref. 2; AAB87707)"
FT /evidence="ECO:0000305"
FT CONFLICT 725..727
FT /note="DPS -> T (in Ref. 2; AAB87707)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="D -> DLN (in Ref. 2; AAB87707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 786 AA; 88301 MW; D9B1CE63502F87C2 CRC64;
MRTYSCLQLV IWTCIFHMVD NSTLQGKDSS HFLRRIVNLK KDEGKMLHRA KRGWMWNQFF
LLEEYTGTDT QYVGKLHTDQ DKGDGNLKYI LTGDGAGNLF VIDENTGDIH AAKRLDREEK
SLYILRAKAI DRKTGRQVEP ESEFIIKIHD INDNEPKFTK DLYTASVPEM SGVGTSVIQV
TATDADDANY GNSAKVVYSI LQGQPYFSVD PESGIIKTAL PDMSRENKEQ YQVVIQAKDM
GGQMGGLSGT TTVNITLTDV NNNPPRFPQS TYQFNSLESA PLGTHLGRIK ANDPDMGENA
ELEYSIAEGE GSDMFDVITD KDTQEGIITV KQNLDFEKKM LYTLRVDASN THPDPRFLHL
GPFKDSAMVK ISVEDVDEPP VFSKLSYLME VDEDVKEGSI IGQVTAYDPD AMNNIIKYSV
DRHTDMDRVF SIHSENGSIF TLKPLDRESS PWHNITITAT EINNPKQSSQ IPVFIRILDI
NDHAPEFATY YETFVCENAK SGQLIQTISV MDKDDPPRGH KFFFEPVPEF PLNPNFTIVD
NKDNTAGIVT RKDGYSRNKM NTYLLPVLIF DNDYPIQSST GTLTIRVCAC DNLGNMQSCN
AEALMLAAGL STGALIAILL CVVILLTLIV LFAALKRQRK KEPLIISKDD VRDNIVTYND
EGGGEEDTQA FDIGTLRNPE AREDSKLRRD VMPETIFQIR RTVPLWENID VQDFIHRRLK
ENDSDPSAPP YDSLATYAYE GNDSVANSLS SLESLTADCN QDYDYLSDWG PRFKKLAEMY
GGNDSD
