PCDB6_HUMAN
ID PCDB6_HUMAN Reviewed; 794 AA.
AC Q9Y5E3; B2R8R9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protocadherin beta-6 {ECO:0000305};
DE Short=PCDH-beta-6 {ECO:0000305};
DE Flags: Precursor;
GN Name=PCDHB6 {ECO:0000312|HGNC:HGNC:8691};
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].
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 [MRNA].
RX PubMed=11322959; DOI=10.1016/s0014-5793(01)02372-9;
RA Vanhalst K., Kools P., Vanden Eynde E., van Roy F.;
RT "The human and murine protocadherin-beta one-exon gene families show high
RT evolutionary conservation, despite the difference in gene number.";
RL FEBS Lett. 495:120-125(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-446; GLN-636 AND
RP ASP-776.
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(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:Q91XZ4}.
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:Q91XZ4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91XZ4};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q91XZ4}.
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:Q91XZ4}.
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DR EMBL; AF152499; AAD43760.1; -; mRNA.
DR EMBL; AF217752; AAK51619.1; -; mRNA.
DR EMBL; AK313482; BAG36266.1; -; mRNA.
DR CCDS; CCDS4248.1; -.
DR RefSeq; NP_001290074.1; NM_001303145.1.
DR RefSeq; NP_061762.2; NM_018939.3.
DR AlphaFoldDB; Q9Y5E3; -.
DR SMR; Q9Y5E3; -.
DR BioGRID; 121070; 34.
DR IntAct; Q9Y5E3; 1.
DR STRING; 9606.ENSP00000231136; -.
DR GlyGen; Q9Y5E3; 4 sites.
DR iPTMnet; Q9Y5E3; -.
DR PhosphoSitePlus; Q9Y5E3; -.
DR BioMuta; PCDHB6; -.
DR DMDM; 13431374; -.
DR jPOST; Q9Y5E3; -.
DR MassIVE; Q9Y5E3; -.
DR PaxDb; Q9Y5E3; -.
DR PeptideAtlas; Q9Y5E3; -.
DR PRIDE; Q9Y5E3; -.
DR ProteomicsDB; 86342; -.
DR Antibodypedia; 27197; 39 antibodies from 10 providers.
DR DNASU; 56130; -.
DR Ensembl; ENST00000231136.4; ENSP00000231136.1; ENSG00000113211.6.
DR GeneID; 56130; -.
DR KEGG; hsa:56130; -.
DR UCSC; uc003lir.4; human.
DR CTD; 56130; -.
DR GeneCards; PCDHB6; -.
DR HGNC; HGNC:8691; PCDHB6.
DR HPA; ENSG00000113211; Low tissue specificity.
DR MIM; 604967; gene.
DR MIM; 606332; gene.
DR neXtProt; NX_Q9Y5E3; -.
DR PharmGKB; PA33040; -.
DR VEuPathDB; HostDB:ENSG00000113211; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q9Y5E3; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q9Y5E3; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9Y5E3; -.
DR SignaLink; Q9Y5E3; -.
DR BioGRID-ORCS; 56130; 11 hits in 1028 CRISPR screens.
DR GenomeRNAi; 56130; -.
DR Pharos; Q9Y5E3; Tdark.
DR PRO; PR:Q9Y5E3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9Y5E3; protein.
DR Bgee; ENSG00000113211; Expressed in cortical plate and 110 other tissues.
DR ExpressionAtlas; Q9Y5E3; baseline and differential.
DR Genevisible; Q9Y5E3; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0009988; P:cell-cell recognition; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS: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 GO; GO:0007416; P:synapse assembly; TAS:UniProtKB.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR032455; Cadherin_C.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT CHAIN 28..794
FT /note="Protocadherin beta-6"
FT /id="PRO_0000003924"
FT TOPO_DOM 28..688
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..794
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT DOMAIN 34..132
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 137..241
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 246..345
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 350..449
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 454..559
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 566..669
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 773..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..101
FT /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT VARIANT 231
FT /note="V -> I (in dbSNP:rs3776096)"
FT /id="VAR_021879"
FT VARIANT 232
FT /note="L -> F (in dbSNP:rs10076554)"
FT /id="VAR_033705"
FT VARIANT 446
FT /note="V -> A (in dbSNP:rs246707)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070665"
FT VARIANT 636
FT /note="H -> Q (in dbSNP:rs246703)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_033706"
FT VARIANT 747
FT /note="Y -> H (in dbSNP:rs17685621)"
FT /id="VAR_033707"
FT VARIANT 776
FT /note="G -> D (in dbSNP:rs17844444)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_070666"
SQ SEQUENCE 794 AA; 87350 MW; A4E84E17896C168D CRC64;
MMQTKVQNKK RQVAFFILLM LWGEVGSESI QYSVLEETES GTFVANLTKD LGLRVGELAS
RGARVVFKGN RQHLQFDPQT HDLLLNEKLD REELCGSTEP CVLPFQVLLE NPLQFFQASL
RVRDINDHAP EFPAREMLLK ISEITMPGKI FPLKMAHDLD TGSNGLQRYT ISSNPHFHVL
TRNRSEGRKF PELVLDKPLD REEQPQLRLT LIALDGGSPP RSGTSEIQIQ VLDINDNVPE
FAQELYEAQV PENNPLGSLV ITVSARDLDA GSFGKVSYAL FQVDDVNQPF EINAITGEIR
LRKALDFEEI QSYDVDVEAT DGGGLSGKCS LVVRVLDVND NAPELTMSFF ISLIPENLPE
ITVAVFSVSD ADSGHNQQVI CSIENNLPFL LRPSVENFYT LVTEGALDRE SRAEYNITIT
VTDLGTPRLK TQQSITVQVS DVNDNVPAFT QTSYTLFVRE NNSPALHIGS VSATDRDSGI
NAQVTYSLLP PQDPHLPLSS LVSINADNGH LFALRSLDYE ALQSFEFRVG ATDRGSPALS
SEALVRLLVL DANDNSPFVL YPLQNGSAPC TELVPRAAEP GYLVTKVVAV DGDSGQNAWL
SYQLLKATEL GLFGVWAHNG EVRTARLLSE RDAAKHRLVV LVKDNGEPPR SATATLHVLL
VDGFSQPYLP LPEAAPAQAQ ADSLTVYLVV ALASVSSLFL FSVLLFVAVR LCRRSRAASV
GRYSVPEGPF PGHLVDVSGT GTLSQSYQYK VCLTGGSETN EFKFLKPIMP NFPPQGTERE
MEETPTSRNS FPFS
