CAD19_HUMAN
ID CAD19_HUMAN Reviewed; 772 AA.
AC Q9H159; B4E1V5; F5H1K0;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cadherin-19;
DE Flags: Precursor;
GN Name=CDH19; Synonyms=CDH7L2; ORFNames=UNQ478/PRO941;
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] (ISOFORM 1).
RX PubMed=10995570; DOI=10.1006/geno.2000.6305;
RA Kools P., Van Imschoot G., van Roy F.;
RT "Characterization of three novel human cadherin genes (CDH7, CDH19, and
RT CDH20) clustered on chromosome 18q22-q23 and with high homology to chicken
RT cadherin-7.";
RL Genomics 68:283-295(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H159-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H159-2; Sequence=VSP_047020, VSP_047021;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, with the exception of
CC uterus.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
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DR EMBL; AJ007607; CAC13126.1; -; mRNA.
DR EMBL; AY358654; AAQ89017.1; -; mRNA.
DR EMBL; AK304000; BAG64917.1; -; mRNA.
DR EMBL; AC090393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS11994.1; -. [Q9H159-1]
DR CCDS; CCDS59325.1; -. [Q9H159-2]
DR RefSeq; NP_001257957.1; NM_001271028.1. [Q9H159-2]
DR RefSeq; NP_066976.1; NM_021153.3. [Q9H159-1]
DR AlphaFoldDB; Q9H159; -.
DR SMR; Q9H159; -.
DR BioGRID; 118390; 29.
DR IntAct; Q9H159; 2.
DR STRING; 9606.ENSP00000262150; -.
DR GlyGen; Q9H159; 8 sites.
DR iPTMnet; Q9H159; -.
DR PhosphoSitePlus; Q9H159; -.
DR BioMuta; CDH19; -.
DR DMDM; 17366818; -.
DR jPOST; Q9H159; -.
DR MassIVE; Q9H159; -.
DR MaxQB; Q9H159; -.
DR PaxDb; Q9H159; -.
DR PeptideAtlas; Q9H159; -.
DR PRIDE; Q9H159; -.
DR ProteomicsDB; 25678; -.
DR ProteomicsDB; 80359; -. [Q9H159-1]
DR Antibodypedia; 23185; 180 antibodies from 24 providers.
DR DNASU; 28513; -.
DR Ensembl; ENST00000262150.7; ENSP00000262150.2; ENSG00000071991.9. [Q9H159-1]
DR Ensembl; ENST00000540086.5; ENSP00000439593.1; ENSG00000071991.9. [Q9H159-2]
DR GeneID; 28513; -.
DR KEGG; hsa:28513; -.
DR MANE-Select; ENST00000262150.7; ENSP00000262150.2; NM_021153.4; NP_066976.1.
DR UCSC; uc002lkc.3; human. [Q9H159-1]
DR CTD; 28513; -.
DR DisGeNET; 28513; -.
DR GeneCards; CDH19; -.
DR HGNC; HGNC:1758; CDH19.
DR HPA; ENSG00000071991; Tissue enhanced (brain, heart muscle).
DR MIM; 603016; gene.
DR neXtProt; NX_Q9H159; -.
DR OpenTargets; ENSG00000071991; -.
DR PharmGKB; PA26292; -.
DR VEuPathDB; HostDB:ENSG00000071991; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000160137; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q9H159; -.
DR OMA; CRYGAFM; -.
DR OrthoDB; 541918at2759; -.
DR PhylomeDB; Q9H159; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; Q9H159; -.
DR SignaLink; Q9H159; -.
DR SIGNOR; Q9H159; -.
DR BioGRID-ORCS; 28513; 5 hits in 1067 CRISPR screens.
DR ChiTaRS; CDH19; human.
DR GenomeRNAi; 28513; -.
DR Pharos; Q9H159; Tbio.
DR PRO; PR:Q9H159; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9H159; protein.
DR Bgee; ENSG00000071991; Expressed in trigeminal ganglion and 172 other tissues.
DR ExpressionAtlas; Q9H159; baseline and differential.
DR Genevisible; Q9H159; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..43
FT /evidence="ECO:0000255"
FT /id="PRO_0000003817"
FT CHAIN 44..772
FT /note="Cadherin-19"
FT /id="PRO_0000003818"
FT TOPO_DOM 44..596
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..148
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 149..256
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 257..370
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 371..470
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 470..581
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 487..490
FT /note="VIQT -> GLFF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047020"
FT VAR_SEQ 491..772
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047021"
FT CONFLICT 141
FT /note="I -> V (in Ref. 3; BAG64917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 87002 MW; 650AD27480343C39 CRC64;
MNCYLLLRFM LGIPLLWPCL GATENSQTKK VKQPVRSHLR VKRGWVWNQF FVPEEMNTTS
HHIGQLRSDL DNGNNSFQYK LLGAGAGSTF IIDERTGDIY AIQKLDREER SLYILRAQVI
DIATGRAVEP ESEFVIKVSD INDNEPKFLD EPYEAIVPEM SPEGTLVIQV TASDADDPSS
GNNARLLYSL LQGQPYFSVE PTTGVIRISS KMDRELQDEY WVIIQAKDMI GQPGALSGTT
SVLIKLSDVN DNKPIFKESL YRLTVSESAP TGTSIGTIMA YDNDIGENAE MDYSIEEDDS
QTFDIITNHE TQEGIVILKK KVDFEHQNHY GIRAKVKNHH VPEQLMKYHT EASTTFIKIQ
VEDVDEPPLF LLPYYVFEVF EETPQGSFVG VVSATDPDNR KSPIRYSITR SKVFNINDNG
TITTSNSLDR EISAWYNLSI TATEKYNIEQ ISSIPLYVQV LNINDHAPEF SQYYETYVCE
NAGSGQVIQT ISAVDRDESI EEHHFYFNLS VEDTNNSSFT IIDNQDNTAV ILTNRTGFNL
QEEPVFYISI LIADNGIPSL TSTNTLTIHV CDCGDSGSTQ TCQYQELVLS MGFKTEVIIA
ILICIMIIFG FIFLTLGLKQ RRKQILFPEK SEDFRENIFQ YDDEGGGEED TEAFDIAELR
SSTIMRERKT RKTTSAEIRS LYRQSLQVGP DSAIFRKFIL EKLEEANTDP CAPPFDSLQT
YAFEGTGSLA GSLSSLESAV SDQDESYDYL NELGPRFKRL ACMFGSAVQS NN
