ID A0A3B3T8Q0_9TELE Unreviewed; 937 AA.
AC A0A3B3T8Q0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Protocadherin alpha-C2-like {ECO:0000313|Ensembl:ENSPKIP00000038828.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000038828.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000038828.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain. {ECO:0000256|ARBA:ARBA00003436}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A3B3T8Q0; -.
DR Ensembl; ENSPKIT00000019824.1; ENSPKIP00000038828.1; ENSPKIG00000016447.1.
DR GeneTree; ENSGT00940000160554; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR032455; Cadherin_C.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF287; CADHERIN-RELATED NEURONAL RECEPTOR VARIABLE 1-RELATED; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_2; 1.
DR Pfam; PF15974; Cadherin_tail; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..937
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017394336"
FT TRANSMEM 696..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..137
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 138..246
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 247..354
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 363..459
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 460..569
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 576..681
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 788..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 937 AA; 102968 MW; AC3983EC6880D57A CRC64;
MADWIMHFVG KNIFISALNL ILLLLCFLDV VSAQFSYSVF EEVEPGTSVG NIAKSLNINV
QDLHSRMFQI VGSSKKKYFD VNLDTGVLYV NDRIDRDMIC SNAPKCTLNV EAMIINPVNI
YRIEINVLDI NDNSPSFRFQ SQTVNITEIT LPGVRFPLLG AYDADSGKNA VKTYKLSPND
HFSLAVHQGG EYSVSADLVL QKALDREKQS TIVLVLTAID GGTPPKSSTS NIIVNILDIN
DNIPAFSRPL YKARIFENAP PGSPVITVNA TDADEGSNGD LVYSFSKHEH DQTLDIFYID
PHTGTITVNG IIDFEIDSDF EIRVQVNDKG QPPMAAHCKV LVEVLDANDN FPEIRVTPLL
DPVKENARVG TVVALVEVTD KDGGQNGIVN CYISNDIPFK LQMNYNNYFS LVINEPLDRE
SSSQYNFTIT ATDEGSPPLS SSSFMIVHIS DINDNPPCFS HLEYSLYLKE NSPAGALIQT
VTASDLDANE NAHLTYSLLD STSKRVPIST MVNINSVTGS IYSLQAFNYE ETKTFQFRVQ
ATDSGVPPLS SNVTVNVFIL DENDNSPQIL PPYSDQGSVN TESIPYSAEA GYFVAKIRAV
DTDSGYNALL SYHISEPKGT NLFRIGTSTG EIRTKRRMSD NDLRTHPLVI LVSDNGDPSL
SSTVSIDVIV TENIEKIQTQ FKERPMKEDR FSSSHLYLLI AIVSVSVIFL LSLITLIALK
CHRTDDTFCR YTAADITTHP DGSWSYSKTS HQYDVCFSSD TLKSDVVVFP VSHAAADTDL
ISINGSDSLR RNQTLPKSEK PKPPSADWRY SASLRAGVKS SVHMEESSVL QGAHGVLVQN
WPTVSSGSGD AEGGEVSPSV GAGMNTNSWQ FRYGPGPGVP QHMKPGEVPE AFLIPGSGAI
ISIRPDQVDD KKDEAKKKKK KKKGKEKKEK GRDDTEQ
//
