ID A0A3Q3BI23_KRYMA Unreviewed; 1160 AA.
AC A0A3Q3BI23;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Protocadherin 9 {ECO:0000313|Ensembl:ENSKMAP00000029490.1};
GN Name=PCDH9 {ECO:0000313|Ensembl:ENSKMAP00000029490.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000029490.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000029490.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_017297289.1; XM_017441800.1.
DR AlphaFoldDB; A0A3Q3BI23; -.
DR Ensembl; ENSKMAT00000029856.1; ENSKMAP00000029490.1; ENSKMAG00000021839.1.
DR GeneTree; ENSGT00940000155079; -.
DR OMA; AYKCPLN; -.
DR OrthoDB; 4259465at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 7.
DR Gene3D; 2.60.40.60; Cadherins; 7.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR013585; Protocadherin.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF248; PROTOCADHERIN-9; 1.
DR Pfam; PF00028; Cadherin; 6.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF08374; Protocadherin; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 7.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 4.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1160
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018598031"
FT TRANSMEM 811..835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..141
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 142..251
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 252..357
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 364..468
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 469..571
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 572..674
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 686..796
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 848..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1160 AA; 127696 MW; A4C7D2F171D29F4E CRC64;
MDLKDYYLLG ALLACIWLDP SIAQELIYPI REELQENVLI GNIPKDLNIS HMNAATGTSA
NLVYRLVSKA GDNPLVRVLS STGEIFTTSN RIDREKLCPG PSFEDSECSF EIEVVILPND
YFRLIKIKII VKDTNDNAPM FPSPVINISI PENTLINSRF AIPSATDPDT GPNSVHKYEL
INGQSAFGLD IVETPEGEKW PQLIVQQNLD REQKDTYVMK IKVEDGGVPQ KSSTAILQVT
VTDVNDNKPV FKESQIEVHI PENSPIGTSV MQLQATDADI GANAEIHYVF GTQVSPATKR
LFALNTTSGL ITVQRPLDRE ETAIHKLSVL ASDGSSSPAR ATVTINVTDV NDNPPNIDLR
YIISPINGTV FLSEKDPINT KIALITVSDK DTDINGKVIC FIEKDVPFHL KAVYDNQYLL
ETSALLDYEG TKEYNFKIVA SDSGKPSLNQ TALVRVRLED ENDNPPIFTQ PVIELAVMEN
NKRDLFLTTL SATDEDSGKN AEIVYQLGPN ASFFDLDRKT GVLTASRVFD REDQDRFLFT
VTARDNGTPP LQTQAAVIVT VLDENDNNPK FTHNHFQFFV SENLPKYSTV GVITVTDSDA
GENAAVSLSI LNDNENFILD PYSGVIKSNV SFDREQQSSY TFDVRAVDSG RPPCSSAAKV
TINVIDVNDN TPIVIYPPSN TSFKLVPLSS IPGSVVAEVF AVDGDTGMNA ELKYTIVSGN
NKGLFRIDPV TGNITLEEKP AVSDIGLHRL VVNISDLGYP KSLHTLVLVF LYVNDTVGNS
SFIYDLIRRT METPIDRNIG ESSETYQSGD YLTIMIAFVT GALVVIIVIF VTVLLRCRHA
SRFKAAQRKK QGAEWMSPNT ENKQNKKKKR KKRKSPKSSL LNFVTIEGNK PDDPAHEPIN
GTISLPTELE EQGIGRFDWN ATPTTTFKPT SPDLARHYKS ASPQSAFHLK ADTPVSVKKH
HVIQELPLDN TFVGGCDTLS KRSSTSSDHF SASESSSQGG FKTKGPMHTR QQAQDDFYEQ
ASPDKRTEAD GNSDPNSDGP LGPRGLVEAT EMCTQECLVL GHSDNCWMPP TLGTYQQPKS
PVSSFGSQRE WGPKDKLLNG HTLSRTWKNE SGRSEHFGDR KQFGSGEGHF SSSGIADIPL
VSLKSCQSAS CPDNPKDQQL
//
