ID A0A2U9CCG2_SCOMX Unreviewed; 1241 AA.
AC A0A2U9CCG2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Putative protocadherin-18-like {ECO:0000313|EMBL:AWP12562.1};
GN ORFNames=SMAX5B_015343 {ECO:0000313|EMBL:AWP12562.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP12562.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP12562.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP026255; AWP12562.1; -; Genomic_DNA.
DR STRING; 52904.ENSSMAP00000024848; -.
DR Proteomes; UP000246464; Chromosome 13.
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; 6.
DR Gene3D; 2.60.40.60; Cadherins; 6.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF9; PROTOCADHERIN-18; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 6.
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:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 713..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..153
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 154..262
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 263..370
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 385..481
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 482..591
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 609..702
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 782..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1005
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 135884 MW; 5CF955FBA7D0E3C6 CRC64;
MEVSARVCAK KMGAKMVQAK GNIFSPALLQ LLLLVALIHG AAGKTLKYKV FEEQKVGTVI
ARLREDVAGV LSKLPSSLNF RFRAMQRGST PLLSVREEDG EISIGTKIDR EKLCEKNLNC
SIEFDVVTLP TEYLQLFHVE VEVLDINDNS PHFSRAIVPI EISESASVGT RVPLDGAVDA
DVGDNSLHTY TLTPNNFFKI DVRTRTDGAK YAELVVMREL DREVLSSYQL QLTASDNGVP
PKSGSTLLKI IISDSNDNSP AFDEQAYIIN LLENSPLGTL IIDLNATDPD EGTNGKIVYS
FSSHVSPKIL ETFKINPETG HITLIKKVDF ETTASYELDV QAQDMGPNSI PGLCKIVVKV
VDVNDNKPEI NINLMTPGKE EVAYISEGAP VDTFIALVRV DDSDAGLNGE VVCRLHGHGH
FRLQKTHEKN YMILTNISLD REKRSEYSLT VIAEDRGSPS LSTIKHFTVQ VLDENDNPPR
FEKSHYEVFK SENNSPGAYL MTVVASDPDL GTNGQVTYNI IDAVVQGSPI STYVTIDPSN
GAIYALRSFD HEDVSRVAFI IQARDGGNPS LSANTTVLLT VLDENDNPPV IHSPPIQNHT
AELLVWKYAS PGQLITALKV TDRDAGANGE LSCAIVGGNE DRLFVMDARR CELRTNATLE
QAPRDVMELK VEVQDRGTSR LSTGALLRLS LQENMDILPP LYPTGTSQAS LDLSLIVIIS
LGAVCALLLI VMVMFATTRC SREKKDPRHN YNCRVAESSY QNHPKKPTRQ IHKADITLVP
TVNGTLPVQA HPRSPSASPT PERGTLGSRQ SHHSRQSLSS LVTISSNHVP ENFALELAHA
TPPVEQVSQL LSMLHQGQYQ PRPSFRGNKY TRSYRYALNE MDKFSLKDSG RGDSEAGDSD
YEPGRESPMD RLLGEGFIEI YAPDGQHRTH AAMRLCTEEC RVLGHSDQCW MPPLASPASS
SSDYRSNLYI PGEEARQVTD HSQEKTPQPC TDTGTARNQS FSTFGKDLGA EDGGEEEGGE
DGGGEAREED LCGTTSLLSE MSSVFQRLLP QGLDSYVQVN EKEKGTSLSG VGVPMTGSLD
RXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX SSHKGSQAPK
NSPQNSGHPP KPHSSPLLTA LVSPTLMQHS PAPVPVPVPL PGPSSKWLPA MEEIPENYEE
DDFDSVLGHL QGKRSDSRHE LVDASELVAE INKLLQDVRQ S
//