PCD18_MOUSE
ID PCD18_MOUSE Reviewed; 1134 AA.
AC Q8VHR0; Q69ZG2; Q80VY4; Q8CB88;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protocadherin 18;
DE Flags: Precursor;
GN Name=Pcdh18; Synonyms=Kiaa1562;
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], INTERACTION WITH DAB1, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Head;
RX PubMed=11716507; DOI=10.1006/bbrc.2001.5998;
RA Homayouni R., Rice D.S., Curran T.;
RT "Disabled-1 interacts with a novel developmentally regulated
RT protocadherin.";
RL Biochem. Biophys. Res. Commun. 289:539-547(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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).
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein.
CC -!- SUBUNIT: Interacts with DAB1. {ECO:0000269|PubMed:11716507}.
CC -!- INTERACTION:
CC Q8VHR0; P97318: Dab1; NbExp=2; IntAct=EBI-399910, EBI-81680;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in kidney and lung.
CC {ECO:0000269|PubMed:11716507}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels throughout the developing
CC embryo, except in the heart and liver. In the developing brain,
CC expressed at high levels in the ventricular zone (vz) in the forebrain
CC and midbrain. Expression in the developing brain is maximal around
CC birth and gradually decreases until it is completely absent from the
CC adult brain. {ECO:0000269|PubMed:11716507}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32482.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF416735; AAL47095.1; -; mRNA.
DR EMBL; AK173204; BAD32482.1; ALT_INIT; mRNA.
DR EMBL; AK036560; BAC29477.1; -; mRNA.
DR EMBL; BC052198; AAH52198.1; -; mRNA.
DR CCDS; CCDS17334.1; -.
DR RefSeq; NP_569715.3; NM_130448.3.
DR AlphaFoldDB; Q8VHR0; -.
DR SMR; Q8VHR0; -.
DR BioGRID; 215816; 2.
DR IntAct; Q8VHR0; 2.
DR STRING; 10090.ENSMUSP00000039245; -.
DR GlyGen; Q8VHR0; 3 sites.
DR iPTMnet; Q8VHR0; -.
DR PhosphoSitePlus; Q8VHR0; -.
DR CPTAC; non-CPTAC-4050; -.
DR PaxDb; Q8VHR0; -.
DR PRIDE; Q8VHR0; -.
DR ProteomicsDB; 294342; -.
DR Antibodypedia; 2719; 104 antibodies from 22 providers.
DR DNASU; 73173; -.
DR Ensembl; ENSMUST00000035931; ENSMUSP00000039245; ENSMUSG00000037892.
DR GeneID; 73173; -.
DR KEGG; mmu:73173; -.
DR UCSC; uc008pdg.2; mouse.
DR CTD; 54510; -.
DR MGI; MGI:1920423; Pcdh18.
DR VEuPathDB; HostDB:ENSMUSG00000037892; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000156295; -.
DR InParanoid; Q8VHR0; -.
DR OMA; CWMPPLL; -.
DR OrthoDB; 64478at2759; -.
DR PhylomeDB; Q8VHR0; -.
DR TreeFam; TF352008; -.
DR BioGRID-ORCS; 73173; 5 hits in 74 CRISPR screens.
DR PRO; PR:Q8VHR0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VHR0; protein.
DR Bgee; ENSMUSG00000037892; Expressed in manus and 220 other tissues.
DR ExpressionAtlas; Q8VHR0; baseline and differential.
DR Genevisible; Q8VHR0; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0007420; P:brain development; IEP:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; NAS:UniProtKB.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR030714; Protocadherin-18.
DR PANTHER; PTHR24028:SF9; PTHR24028:SF9; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_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; 6.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1134
FT /note="Protocadherin 18"
FT /id="PRO_5000061325"
FT TOPO_DOM 28..699
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..1134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..137
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 138..246
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 247..354
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 361..465
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 466..576
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 582..688
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 769..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..1134
FT /note="Interaction with DAB1"
FT /evidence="ECO:0000269|PubMed:11716507"
FT REGION 941..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 650
FT /note="A -> T (in Ref. 1; AAL47095, 2; BAD32482 and 4;
FT AAH52198)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="S -> N (in Ref. 2; BAD32482 and 4; AAH52198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1134 AA; 125420 MW; 6C99B12BCA420353 CRC64;
MHQMNTKMHF RFALALLMAF FSHDVLAKNL KYRIYEEQRV GSVIARLSED VADVLLKLPN
PSAVRFRAMP RGNSPLLVVN ENTGEISIGA KIDREQLCQK NLNCSIEFDV LTLPTEHLQL
FHIEVDVLDI NDNSPQFSRP VIPIEISESA AVGTRIPLDS AFDPDVGENS LHTYSLSAND
YFNIEVRTRT DGAKYAELIV VKELDRELKA SYELQLTASD MGVPQRSGSS ILKISISDSN
DNSPAFEQPS YTIQLLENSP VGTLLLDLNA TDPDEGANGR IVYSFSSHVS PKIIETFKID
SEKGHLTLFK PVDYEITKSY EIDVQAQDLG PNSIPAHCKI IIKVVDVNDN KPEISINLMS
PGKEEVSYVF EGDPIDTFVA IVRVQDKDSG LNGEIICKLH GHGHFKLQKT YENNYLILTN
ATLDREKRSE YSLTVIAEDK GTPSLSSVRH FTVQINDIND NPPRFQRSRY EFVISENNSP
GAYITTVTAT DPDLGENGHV TYTILESFVL GSSITTYVTI DPSNGAIYAL RIFDHEEVSQ
ITFVVEARDG GSQKQLSSNT TVVLTIIDEN DNVPVVIGPA MHNNTAEISI PKGAESGFHV
TRIRVVDRDS GANAEFSCSI VSGNEENIFI MDPRSCDIHT NVSMESIPSA EWALSVIIQD
KGSPPLHTKV LLRCMVFDYA ESVTSTAMTS VSRASLDVSM IIIISLGAIC AVLLVIMVLF
ATRCNREKKD TRSYNCRVAE STYQHHPKRP SRQIHKGDIT LVPTINGTLP IRSHHRSSPS
SSPTLERGQM GSRQSHNSHQ SLNSLVTISS NHVPENFSLE LTHATPAVEV SQLLSMLHQG
QYQPRPSFRG NKYSRSYRYA LQDMDKFSLK DSGRGDSEAG DSDYDLGRDS PIDRLLGEGF
SDLFLTDGRI PAAMRLCTEE CRVLGHSDQC WMPPLPSPSS DYRSNMFIPG EEFPAQPQQQ
HSHQGLDDDS QPAENGEKKK SFSTFGKDSP SDEDSGDSST SSLLSEMSSV FQRLLPASLD
TFSECNEGDR SNSLERRKGP AQGKTGGYPQ GVAAWAASTH FQNPTSSSGT PLGTHSSVQP
SSKWLPAMEE IPENYEEDDF DNVLNHLSDG KHELMDASEL VAEINKLLQD VRQS
