PCDA7_HUMAN
ID PCDA7_HUMAN Reviewed; 937 AA.
AC Q9UN72; O75282;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Protocadherin alpha-7 {ECO:0000305};
DE Short=PCDH-alpha-7 {ECO:0000305};
DE Flags: Precursor;
GN Name=PCDHA7 {ECO:0000312|HGNC:HGNC:8673};
GN Synonyms=CNRS4 {ECO:0000312|HGNC:HGNC:8673};
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 [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=10380929; DOI=10.1016/s0092-8674(00)80789-8;
RA Wu Q., Maniatis T.;
RT "A striking organization of a large family of human neural cadherin-like
RT cell adhesion genes.";
RL Cell 97:779-790(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein involved in cells
CC self-recognition and non-self discrimination. Thereby, it is involved
CC in the establishment and maintenance of specific neuronal connections
CC in the brain. {ECO:0000250|UniProtKB:Q91Y13}.
CC -!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
CC different cells). Forms promiscuous heterodimers in cis (at the plasma
CC membrane of the same cell) with other protocadherins.
CC {ECO:0000250|UniProtKB:Q91Y13}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91Y13};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q91Y13}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UN72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UN72-2; Sequence=VSP_000684, VSP_000685;
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. This is a head-to-tail interaction, the cadherin
CC 1 domain interacting with the cadherin 4 domain and the cadherin 2
CC domain interacting the cadherin 3 domain of the other protocadherin.
CC The cadherin 6 domain mediates promiscuous interactions with
CC protocadherins on the same cell membrane. Each cadherin domain binds
CC three calcium ions. {ECO:0000250|UniProtKB:Q91Y13}.
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DR EMBL; AF152315; AAD43709.1; -; mRNA.
DR EMBL; AF152485; AAD43746.1; -; mRNA.
DR EMBL; AC005609; AAC34319.1; -; Genomic_DNA.
DR CCDS; CCDS54918.1; -. [Q9UN72-1]
DR RefSeq; NP_061733.1; NM_018910.2. [Q9UN72-1]
DR RefSeq; NP_114040.1; NM_031852.1. [Q9UN72-2]
DR AlphaFoldDB; Q9UN72; -.
DR SMR; Q9UN72; -.
DR BioGRID; 121081; 26.
DR IntAct; Q9UN72; 5.
DR STRING; 9606.ENSP00000436426; -.
DR GlyGen; Q9UN72; 3 sites.
DR iPTMnet; Q9UN72; -.
DR PhosphoSitePlus; Q9UN72; -.
DR BioMuta; PCDHA7; -.
DR DMDM; 13878422; -.
DR EPD; Q9UN72; -.
DR jPOST; Q9UN72; -.
DR MassIVE; Q9UN72; -.
DR PaxDb; Q9UN72; -.
DR PeptideAtlas; Q9UN72; -.
DR PRIDE; Q9UN72; -.
DR ProteomicsDB; 85259; -. [Q9UN72-1]
DR ProteomicsDB; 85260; -. [Q9UN72-2]
DR Antibodypedia; 27161; 102 antibodies from 15 providers.
DR DNASU; 56141; -.
DR Ensembl; ENST00000356878.5; ENSP00000349344.5; ENSG00000204963.6. [Q9UN72-2]
DR Ensembl; ENST00000525929.2; ENSP00000436426.1; ENSG00000204963.6. [Q9UN72-1]
DR GeneID; 56141; -.
DR KEGG; hsa:56141; -.
DR MANE-Select; ENST00000525929.2; ENSP00000436426.1; NM_018910.3; NP_061733.1.
DR UCSC; uc003lhq.2; human. [Q9UN72-1]
DR CTD; 56141; -.
DR DisGeNET; 56141; -.
DR GeneCards; PCDHA7; -.
DR HGNC; HGNC:8673; PCDHA7.
DR HPA; ENSG00000204963; Tissue enhanced (brain).
DR MIM; 604966; gene.
DR MIM; 606313; gene.
DR neXtProt; NX_Q9UN72; -.
DR OpenTargets; ENSG00000204963; -.
DR PharmGKB; PA33019; -.
DR VEuPathDB; HostDB:ENSG00000204963; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000163312; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q9UN72; -.
DR OMA; QECISID; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q9UN72; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9UN72; -.
DR SignaLink; Q9UN72; -.
DR SIGNOR; Q9UN72; -.
DR BioGRID-ORCS; 56141; 7 hits in 1018 CRISPR screens.
DR GenomeRNAi; 56141; -.
DR Pharos; Q9UN72; Tbio.
DR PRO; PR:Q9UN72; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UN72; protein.
DR Bgee; ENSG00000204963; Expressed in cortical plate and 55 other tissues.
DR Genevisible; Q9UN72; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0009988; P:cell-cell recognition; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
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; 5.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Membrane; Metal-binding; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..937
FT /note="Protocadherin alpha-7"
FT /id="PRO_0000003896"
FT TOPO_DOM 30..697
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91Y13"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..937
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91Y13"
FT DOMAIN 30..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 134..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 581..678
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..795
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 814..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 846..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..899
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 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..102
FT /evidence="ECO:0000250|UniProtKB:Q91Y13"
FT VAR_SEQ 786..789
FT /note="PRQP -> VSHK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10380929"
FT /id="VSP_000684"
FT VAR_SEQ 790..937
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10380929"
FT /id="VSP_000685"
FT VARIANT 138
FT /note="R -> K (in dbSNP:rs10067182)"
FT /id="VAR_048527"
FT VARIANT 663
FT /note="A -> G (in dbSNP:rs6880234)"
FT /id="VAR_048528"
SQ SEQUENCE 937 AA; 100865 MW; 1BBF0D4DF89BCD8D CRC64;
MVCPNGYDPG GRHLLLFIII LAAWEAGRGQ LHYSVPEEAK HGNFVGRIAQ DLGLELAELV
PRLFRAVCKF RGDLLEVNLQ NGILFVNSRI DREELCGRSA ECSIHLEVIV ERPLQVFHVD
VEVKDINDNP PVFPATQRNL FIAESRPLDS RFPLEGASDA DIGENALLTY RLSPNEYFFL
DVPTSNQQVK PLGLVLRKLL DREETPELHL LLTATDGGKP ELTGTVQLLI TVLDNNDNAP
VFDRTLYTVK LPENVSIGTL VIHPNASDLD EGLNGDIIYS FSSDVSPDIK SKFHMDPLSG
AITVIGHMDF EESRAHKIPV EAVDKGFPPL AGHCTVLVEV VDVNDNAPQL TLTSLSLPIP
EDAQPGTVIT LISVFDRDFG VNGQVTCSLT PRVPFKLVST FKNYYSLVLD SALDRESVSA
YELVVTARDG GSPSLWATAS VSVEVADVND NAPAFAQPEY TVFVKENNPP GCHIFTVSAG
DADAQKNALV SYSLVELRVG ERALSSYVSV HAESGKVYAL QPLDHEELEL LQFQVSARDA
GVPPLGSNVT LQVFVLDEND NAPALLAPRV GGTGGAVREL VPRSVGAGHV VAKVRAVDAD
SGYNAWLSYE LQPVAAGASI PFRVGLYTGE ISTTRALDET DAPRHRLLVL VKDHGEPSLT
ATATVLVSLV ESGQAPKASS RASLGIAGPE TELVDVNVYL IIAICAVSSL LVLTLLLYTA
LRCSAPSSEG ACSLVKPTLV CSSAVGSWSF SQQRRQRVCS GEGPPKTDLM AFSPSLPQGP
SSTDNPRQPN PDWRYSASLR AGMHSSVHLE EAGILRAGPG GPDQQWPTVS SATPEPEAGE
VSPPVGAGVN SNSWTFKYGP GNPKQSGPGE LPDKFIIPGS PAIISIRQEP TNSQIDKSDF
ITFGKKEETK KKKKKKKGNK TQEKKEKGNS TTDNSDQ
