CAD16_RABIT
ID CAD16_RABIT Reviewed; 829 AA.
AC Q28634;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Cadherin-16;
DE AltName: Full=Kidney-specific cadherin;
DE Short=Ksp-cadherin;
DE Flags: Precursor;
GN Name=CDH16;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 570-586.
RC STRAIN=New Zealand white;
RX PubMed=7615566; DOI=10.1074/jbc.270.29.17594;
RA Thomson R.B., Igarashi P., Biemesderfer D., Kim R., Abu-Alfa A.,
RA Soleimani M., Aronson P.S.;
RT "Isolation and cDNA cloning of Ksp-cadherin, a novel kidney-specific member
RT of the cadherin multigene family.";
RL J. Biol. Chem. 270:17594-17601(1995).
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 -!- TISSUE SPECIFICITY: Kidney specific. Limited to the basolateral
CC membranes of renal tubular epithelial cells.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U28945; AAC48472.1; -; mRNA.
DR PIR; I46536; I46536.
DR RefSeq; NP_001164517.1; NM_001171046.1.
DR AlphaFoldDB; Q28634; -.
DR SMR; Q28634; -.
DR STRING; 9986.ENSOCUP00000000506; -.
DR GeneID; 100328594; -.
DR KEGG; ocu:100328594; -.
DR CTD; 1014; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q28634; -.
DR OrthoDB; 190556at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR InterPro; IPR030721; Cadherin-16.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR PANTHER; PTHR24028:SF1; PTHR24028:SF1; 1.
DR Pfam; PF00028; Cadherin; 3.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Direct protein sequencing;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..829
FT /note="Cadherin-16"
FT /id="PRO_0000003811"
FT TOPO_DOM 19..786
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 808..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..126
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 131..235
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 242..336
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 341..449
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 455..564
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 569..665
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 666..786
FT /note="Ectodomain G"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 829 AA; 88828 MW; D2DF10E6C47A43B9 CRC64;
MVPAWLWLLC FSVPQALVEV SPTTLHVEVP ENYGGNFPLY LTKLPWPHKE AGGRVVLSGD
SGVAAEGPFS VEAESGFLLV TRALDREEQA EYQIQVTLEA EDGHVLWGPQ SVTVHVKDEN
DQVPQFSQAL YSARLSQGTR PGVPFLFLEA SDGDEPGTAN SDLRFHILSQ TPAQPSPDVF
RLEPRLGALA LSPEGSAGFD HALEGPYQLL VQVKDMGDQA SGHQATATVE ISIVESTWTP
LEPVHLAENL KVPYPHHLAQ VHWSGGDVHY RLESQPPGPF DVDTEGKLYV TGELDREAQE
QYVLQVQAQN SRGEDYAEPL ELHVVVTDEN DHAPVCPPRG PPVSVPELSP PGTAVTTLSA
EDADAPGSPN SHVVYRLLSP EPQEGPEGGA FQLDPTSGSV SLGAAPLEAG QNMLLQVLAV
DLAGAEAGLS STCEVAVTVT DVNDHAPEFT SSQVGPVSLP EDTEPGTLVA TLTATDADLE
PAFRLMDFTI EAGDGEGTFG LDWEPDSGHV QLYLLKNLSY EAAPSHTVVV VVRNVVETVG
PGPGPGATAT VTVLVEKVMP PPRLEQKSYE ADIPVNAPAG SFLLTIQPAE PWNGALRFSL
VNDSEGWFCI QKVSGEVHTA RPLQGARPGD SYTVLVEAQD ADAPRLSTSA ALVIHFLRAP
PAPALPLAPM PSRHLCTPRQ DHGVLIPAPS EDPDMATGHG PYSFALGPNP TVQRDWRLQP
LNDSHAFLTL ALHWVEPREH IVPVVVSQDA RVWQLPVRVV VCRCNTEGEC MRKVGRMKGM
PTKLSAVGIL VGTLAAIGFF LILIFTHLAL ARKKDLDAPA DNVPLKAAA
