PCDA7_MOUSE
ID PCDA7_MOUSE Reviewed; 937 AA.
AC Q91Y13;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Protocadherin alpha-7 {ECO:0000305};
DE Short=PCDH-alpha-7 {ECO:0000305};
DE Flags: Precursor;
GN Name=Pcdha7 {ECO:0000312|MGI:MGI:1298369};
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=11230163; DOI=10.1101/gr.167301;
RA Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J., Dickson M.,
RA Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
RT "Comparative DNA sequence analysis of mouse and human protocadherin gene
RT clusters.";
RL Genome Res. 11:389-404(2001).
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 X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 30-560 OF HOMODIMER IN COMPLEX
RP WITH CALCIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN,
RP DISULFIDE BONDS, GLYCOSYLATION AT THR-223; THR-225; ASN-257; ASN-265;
RP THR-438; SER-478 AND ASN-548, AND MUTAGENESIS OF LYS-138; ASP-284 AND
RP PRO-328.
RX PubMed=27161523; DOI=10.1016/j.neuron.2016.04.004;
RA Goodman K.M., Rubinstein R., Thu C.A., Bahna F., Mannepalli S., Ahlsen G.,
RA Rittenhouse C., Maniatis T., Honig B., Shapiro L.;
RT "Structural basis of diverse homophilic recognition by clustered alpha- and
RT beta-protocadherins.";
RL Neuron 90:709-723(2016).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein involved in cells
CC self-recognition and non-self discrimination (PubMed:27161523).
CC Thereby, it is involved in the establishment and maintenance of
CC specific neuronal connections in the brain (PubMed:27161523).
CC {ECO:0000269|PubMed:27161523}.
CC -!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
CC different cells) (PubMed:27161523). Forms promiscuous heterodimers in
CC cis (at the plasma membrane of the same cell) with other protocadherins
CC (PubMed:27161523). {ECO:0000269|PubMed:27161523}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27161523};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:27161523}.
CC -!- DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-
CC interaction, the interaction with an identical protocadherin expressed
CC by a neighboring cell (PubMed:27161523). This is a head-to-tail
CC interaction, the cadherin 1 domain interacting with the cadherin 4
CC domain and the cadherin 2 domain interacting the cadherin 3 domain of
CC the other protocadherin (PubMed:27161523). The cadherin 6 domain
CC mediates promiscuous interactions with protocadherins on the same cell
CC membrane. Each cadherin domain binds three calcium ions
CC (PubMed:27161523). {ECO:0000269|PubMed:27161523, ECO:0000312|PDB:5DZV}.
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DR EMBL; AY013765; AAK26054.1; -; mRNA.
DR EMBL; AC020968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_034087.1; NM_009957.1.
DR PDB; 5DZV; X-ray; 3.60 A; A/B=30-560.
DR PDBsum; 5DZV; -.
DR AlphaFoldDB; Q91Y13; -.
DR SMR; Q91Y13; -.
DR CORUM; Q91Y13; -.
DR GlyGen; Q91Y13; 7 sites.
DR iPTMnet; Q91Y13; -.
DR PhosphoSitePlus; Q91Y13; -.
DR PRIDE; Q91Y13; -.
DR ProteomicsDB; 289321; -.
DR DNASU; 12939; -.
DR Ensembl; ENSMUST00000192631; ENSMUSP00000142156; ENSMUSG00000104318.
DR GeneID; 12939; -.
DR KEGG; mmu:12939; -.
DR UCSC; uc008epc.3; mouse.
DR CTD; 56141; -.
DR MGI; MGI:1298369; Pcdha7.
DR VEuPathDB; HostDB:ENSMUSG00000104318; -.
DR GeneTree; ENSGT00940000163312; -.
DR HOGENOM; CLU_006480_0_0_1; -.
DR OMA; GINREIC; -.
DR OrthoDB; 300321at2759; -.
DR BioGRID-ORCS; 12939; 2 hits in 64 CRISPR screens.
DR PRO; PR:Q91Y13; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91Y13; protein.
DR Bgee; ENSMUSG00000104318; Expressed in thoracic ganglion and 51 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0009988; P:cell-cell recognition; IDA:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF15974; Cadherin_tail; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..937
FT /note="Protocadherin alpha-7"
FT /evidence="ECO:0000255"
FT /id="PRO_5008429382"
FT TOPO_DOM 30..697
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:27161523"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..937
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27161523"
FT DOMAIN 34..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 157..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..350
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 351..455
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 456..565
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 587..682
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 774..777
FT /note="PXXP 1"
FT REPEAT 786..789
FT /note="PXXP 2"
FT REPEAT 819..822
FT /note="PXXP 3"
FT REPEAT 860..863
FT /note="PXXP 4"
FT REPEAT 878..881
FT /note="PXXP 5"
FT REGION 755..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..881
FT /note="5 X 4 AA repeats of P-X-X-P"
FT REGION 816..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 223
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZV"
FT CARBOHYD 225
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZV"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZV"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZV"
FT CARBOHYD 438
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZV"
FT CARBOHYD 478
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZV"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZV"
FT DISULFID 96..102
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZV"
FT MUTAGEN 138
FT /note="K->Q: Changed homophilic interaction, being unable
FT to interact with the wild-type protein but able to bind
FT itself; when associated with L-284."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 284
FT /note="D->L: No effect on homophilic interaction. Changed
FT homophilic interaction, being unable to interact with the
FT wild-type protein but able to bind itself; when associated
FT with Q-138."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 328
FT /note="P->F: Changed homophilic interaction, being unable
FT to interact with the wild-type protein but able to bind
FT itself."
FT /evidence="ECO:0000269|PubMed:27161523"
SQ SEQUENCE 937 AA; 101266 MW; E90ED1036C6E215A CRC64;
MVNLRGYNWK SQQLLLFLII VAAWEAGSGQ LHYSVPEEAK HGTFVGRIAQ DLGLELTELV
PRLFRVASKD RGDLLEVNLQ NGILFVNSRI DREELCGRSA ECSIHLEVIV DRPLQVFHVE
VEVKDINDNP PMFPATQKAL FILESRLLDS RFPLEGASDA DVGSNALLTY RLSTNEHFSL
DVPPNHEQVK PLGLVLRKPL DREEAAEIRL LLTATDGGKP ELTGTVQLLI TVLDVNDNAP
VFDRSLYTVK LPENVPNGTL VIKVNASDLD EGVNGDVMYS FSSDVSSDIK SKFHMDTVSG
EITVIGIIDF EESKAYKIPL EARDKGFPQL PGHCTILVEV VDANDNAPQL TVSSLSLPVS
EDSQPGRVVT LISVFDRDSG ANGQVTCSLT PHIPFKLVST FKNYYSLVLD SALDRETIAN
YDVIVTARDG GSPSLWATAS VSVEVADVND NAPLFAQPEY TVFVKENNPP GAHIFTVSAM
DADAQENALV SYSLVERRVG ERLLSSYVSV HAESGKVFAL QPLDHEELEL LQFQVSARDA
GVPALGSNVT LQVFVLDEND NAPTLLGPLA NGVGGTMNEV VSRALVPGQV VAKVRAVDED
SGYNAWLSFE LQPVAGGVRS PFRVGLYTGE ISTTRALEET DALRQCLLVL VKDHGEPSLT
ATATVLLSLV DSGQTQKVSS KVSAGASRVD QRLVDVNVYL IIAICAVSSL LVLTLLLYTA
LRCSATPTDG ACAPGKPMLV CSSAVGSWSY SQQRRQRVCS GEGPPKTDLM AFSPSLPQGP
SSTDNPRQPN PDWRYSASLR AGMHSSVHLE EAGILRAGPG GPDQQWPTVS SATPEPEAGE
VSPPVGAGVN SNSWTFKYGP GNPKQSGPGE LPDKFIIPGS PAIISIRQEP ANNQIDKSDF
ITFGKKEETK KKKKKKKGNK TQEKKEKGNS TTDNSDQ
