CAD19_HUMAN » Cadherin-19

CAD19_HUMAN » Cadherin-19
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
CAD19_HUMAN » Cadherin-19 »
Hydrophobic Thickness 31.2 ± 1.8 Å
Tilt Angle 1 ± 2°
ΔGtransfer -57.1 kcal/mol
ΔGfold -24.0 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 596-620 (596-623)
Pathways none
PDB none
OPM none
Complexes none
Interactions

CADH6, Complex: CADH6:CAD19, PubMed

Domains

AA: 48-139, PDBID: 1ZVN, Subunit A, Seq Identity:55%, Cadherin domain

AA: 153-247, PDBID: 2A4E, Subunit A, Seq Identity:66%, Cadherin domain

AA: 261-362, PDBID: 2A62, Subunit A, Seq Identity:35%, Cadherin domain

AA: 375-461, PDBID: 2WCP, Subunit A, Seq Identity:30%, Cadherin domain

AA: 474-571, PDBID: 2O72, Subunit A, Seq Identity:23%, Cadherin domain

AA: 619-767, PDBID: 1I7W, Subunit B, Seq Identity:40%, Cadherin cytoplasmic region

UniProt annotation for CAD19_HUMAN » Cadherin-19
FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.

TISSUE SPECIFICITY: Expressed in many tissues, with the exception of uterus.

DOMAIN: Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.

UniProt features for CAD19_HUMAN » Cadherin-19
SIGNAL 1 21 Potential.
PROPEP 22 43 Potential.
CHAIN 44 772 Cadherin-19.
DOMAIN 44 148 Cadherin 1.
DOMAIN 149 256 Cadherin 2.
DOMAIN 257 370 Cadherin 3.
DOMAIN 371 470 Cadherin 4.
DOMAIN 470 581 Cadherin 5.
Amino Acid Sequence for CAD19_HUMAN » Cadherin-19
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