CDHR2_MOUSE
ID CDHR2_MOUSE Reviewed; 1308 AA.
AC E9Q7P9; B7ZP46; B9EJ32; Q3UN77;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cadherin-related family member 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=Cdhr2 {ECO:0000312|MGI:MGI:2687323};
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Intestinal mucosa;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1297, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH USH1C.
RX PubMed=26812017; DOI=10.1016/j.devcel.2015.12.020;
RA Li J., He Y., Lu Q., Zhang M.;
RT "Mechanistic basis of organization of the Harmonin/USH1C-mediated brush
RT border microvilli tip-link complex.";
RL Dev. Cell 36:179-189(2016).
CC -!- FUNCTION: Intermicrovillar adhesion molecule that forms, via its
CC extracellular domain, calcium-dependent heterophilic complexes with
CC CDHR5 on adjacent microvilli. Thereby, controls the packing of
CC microvilli at the apical membrane of epithelial cells. Through its
CC cytoplasmic domain, interacts with microvillus cytoplasmic proteins to
CC form the intermicrovillar adhesion complex/IMAC. This complex plays a
CC central role in microvilli and epithelial brush border differentiation.
CC May also play a role in cell-cell adhesion and contact inhibition in
CC epithelial cells. {ECO:0000250|UniProtKB:Q9BYE9}.
CC -!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion
CC complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B,
CC USH1C, CDHR2 and CDHR5. Interacts with MAST2 (By similarity). Interacts
CC (via cytoplasmic domain) with USH1C and MYO7B; required for proper
CC localization of CDHR2 to microvilli tips and its function in brush
CC border differentiation (Probable). {ECO:0000250|UniProtKB:Q9BYE9,
CC ECO:0000305|PubMed:26812017}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9BYE9}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9BYE9}. Cell projection, microvillus membrane
CC {ECO:0000250|UniProtKB:Q9BYE9}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9BYE9}. Cell junction
CC {ECO:0000250|UniProtKB:Q9BYE9}.
CC -!- DOMAIN: The cadherin 1 domain is required for binding to CDHR5.
CC {ECO:0000250|UniProtKB:Q9BYE9}.
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DR EMBL; AK144400; BAE25870.1; -; mRNA.
DR EMBL; AC162526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141301; AAI41302.1; -; mRNA.
DR EMBL; BC145624; AAI45625.1; -; mRNA.
DR CCDS; CCDS36669.1; -.
DR RefSeq; NP_001028536.2; NM_001033364.3.
DR PDB; 5CYX; X-ray; 2.10 A; A=21-348.
DR PDBsum; 5CYX; -.
DR AlphaFoldDB; E9Q7P9; -.
DR SMR; E9Q7P9; -.
DR STRING; 10090.ENSMUSP00000043596; -.
DR iPTMnet; E9Q7P9; -.
DR PhosphoSitePlus; E9Q7P9; -.
DR jPOST; E9Q7P9; -.
DR MaxQB; E9Q7P9; -.
DR PaxDb; E9Q7P9; -.
DR PRIDE; E9Q7P9; -.
DR ProteomicsDB; 280036; -.
DR Antibodypedia; 2236; 41 antibodies from 11 providers.
DR Ensembl; ENSMUST00000037145; ENSMUSP00000043596; ENSMUSG00000034918.
DR GeneID; 268663; -.
DR KEGG; mmu:268663; -.
DR UCSC; uc007qoz.2; mouse.
DR CTD; 54825; -.
DR MGI; MGI:2687323; Cdhr2.
DR VEuPathDB; HostDB:ENSMUSG00000034918; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000161160; -.
DR HOGENOM; CLU_005755_0_0_1; -.
DR InParanoid; E9Q7P9; -.
DR OMA; TIQAYDN; -.
DR OrthoDB; 83119at2759; -.
DR PhylomeDB; E9Q7P9; -.
DR TreeFam; TF332908; -.
DR BioGRID-ORCS; 268663; 1 hit in 73 CRISPR screens.
DR PRO; PR:E9Q7P9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; E9Q7P9; protein.
DR Bgee; ENSMUSG00000034918; Expressed in small intestine Peyer's patch and 42 other tissues.
DR Genevisible; E9Q7P9; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031528; C:microvillus membrane; ISS:UniProtKB.
DR GO; GO:0044214; C:spanning component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0090675; P:intermicrovillar adhesion; ISS:UniProtKB.
DR GO; GO:0060243; P:negative regulation of cell growth involved in contact inhibition; ISS:UniProtKB.
DR GO; GO:0032532; P:regulation of microvillus length; ISS:UniProtKB.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 7.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 9.
DR SUPFAM; SSF49313; SSF49313; 9.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Differentiation; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1308
FT /note="Cadherin-related family member 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5003243107"
FT TOPO_DOM 21..1152
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1153..1173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1174..1308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 33..124
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 125..241
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 242..353
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 368..480
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 481..586
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 586..695
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 695..807
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 809..927
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 929..1051
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 1178..1308
FT /note="Mediates interaction with USH1C and MYO7B and is
FT required for proper localization to microvilli tips and
FT function in microvilli organization"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE9"
FT REGION 1251..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYE9"
FT MOD_RES 1297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 371
FT /note="N -> D (in Ref. 1; BAE25870)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="Q -> QS (in Ref. 3; AAI41302/AAI45625)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="W -> C (in Ref. 3; AAI45625)"
FT /evidence="ECO:0000305"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5CYX"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5CYX"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:5CYX"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:5CYX"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:5CYX"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:5CYX"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:5CYX"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 276..285
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:5CYX"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:5CYX"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 314..325
FT /evidence="ECO:0007829|PDB:5CYX"
FT STRAND 334..343
FT /evidence="ECO:0007829|PDB:5CYX"
SQ SEQUENCE 1308 AA; 142633 MW; 9C1DD3E53E556A0A CRC64;
MAWLWLLCAL LPAFMVSVTA NSPPSFGVNM TLVTLPEDLP VGAVAFWLVA TDSDNDHLTY
GISGPNASYF SVNANTGEVK LASPLDFETV PFFKITISTS DGLNIRTAEM QVIVEDRNDN
IPVFLNTEFS TSINETLPVG SVVFSVLAED KDTGTAGLVQ YFIEKVIPST ANSNNLFRIL
ENGSIVLNDT LSYNNKSAFY QLELKACDSG GILDNKPKTQ CSQPVFVSIS VIDEPDLDPR
FIREFYSASV AEDATLGTSV LTVEAVDSDK GINDIVTYSV SNSTRPGWFD IREDGVIFVN
GSLDREQLLL ENEEVQIQVT ATEKNLNIYG QEAKASMWVT IRVTDVNDHK PEFYNCSLPG
CSFSPQEAQV NFIGYVDEHA SARISIDGLT MVAYDPDQGD NGTFLLSLNG QDAEAFNVSP
ERAAGSVSVQ VVVRNSEMVD YEKETVMVVE VVATDSVSNN YSVATVTIHL RNINDHRPVF
SQSLYELTVP EHCPTGYLVT DKIQATDLDG DEWGPITYSL LPGNGADLFE VEPNSGNLTV
KNGTLLDREK QAVYYLTLQA TDGGNQSTTT ALEITLLDIN DNPPVVRGSY NVFVPEENGN
VSVTIQAYDD DQPDTNNSLL VFSLLPGPYS SNFSLDPNTG LLRNLGPLDR EAIDPALEGR
IVLTVIVADC GEPSLSTNVN VTITVEDIND NLPVFNQSYE FSVWERVPGA WVGTVKAWDA
DQTAANNRIS FSLSGTGANN FILQGNVLEQ GWAEGSLWLL PDVRLDYETQ KFFHLTVSAE
NPGPQGLDST ANVTVTVMDV NDEPPTLDAA SLQAISVTEN GSEHGQVTRV IAQDVDTAAL
LRIELVDVIC TKAGVDVGSV CHGWFSVDGN GSVYINQSEA IDYEACHLVT LVVRAYDLNT
DPGFDAYSSN GSLLINIKDK NDNAPYFLPN NQTFVIIPEL VLPNQQVASV QARDEDSEDN
GIIMFSILKA EFVRKDGTSN PVQVFRITRS VEAGLFTGSI ELVTNLDSTI QGTYQVTVQA
QDQPTLGPAL ETQTTLNLFT VDQSYRVRLQ FSTSKEDVGA NMEEIKEALI QATRTSVYVV
TIQNIDSTAR ARASSYMDAY FVFSNGTALT LTELNMMIRK DQDALRQLLQ LGLVVVSSQE
SQEPDQQKLL TSVIIGLVVS LVLVLVILIT ALVCLRKSYH RKLRAMKAGK EARKTPIETT
APTAAIPGTN MYNTDRANPV LDLPTKDLGL ECHSSSDLDY DSLNSLDENS VDLDMDSKEF
KRKDLPGDPP EPDPEPLTAV LSGRSAGASE QQKKNLSFTN PGLDTTDL
