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   24-JAN-2024, entry version 149.
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.ENSMUSP00000154022; -.
DR   GlyConnect; 2173; 2 N-Linked glycans (2 sites).
DR   GlyCosmos; P70407; 5 sites, 2 glycans.
DR   GlyGen; P70407; 5 sites, 2 N-linked glycans (2 sites).
DR   iPTMnet; P70407; -.
DR   PhosphoSitePlus; P70407; -.
DR   PaxDb; 10090-ENSMUSP00000026432; -.
DR   ProteomicsDB; 281745; -.
DR   AGR; MGI:107433; -.
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:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; 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: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 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   CDD; cd11304; Cadherin_repeat; 5.
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; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF99; CADHERIN-9; 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   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
//