GenomeNet

Database: UniProt
Entry: A0A3Q3ARV1_KRYMA
LinkDB: A0A3Q3ARV1_KRYMA
Original site: A0A3Q3ARV1_KRYMA 
ID   A0A3Q3ARV1_KRYMA        Unreviewed;      1000 AA.
AC   A0A3Q3ARV1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Protocadherin alpha-C2-like {ECO:0000313|Ensembl:ENSKMAP00000014174.1};
GN   Name=PCDHAC2 {ECO:0000313|Ensembl:ENSKMAP00000014174.1};
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:ENSKMAP00000014174.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000014174.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_017268055.1; XM_017412566.1.
DR   AlphaFoldDB; A0A3Q3ARV1; -.
DR   Ensembl; ENSKMAT00000014385.1; ENSKMAP00000014174.1; ENSKMAG00000010638.1.
DR   GeneID; 108233861; -.
DR   KEGG; kmr:108233861; -.
DR   GeneTree; ENSGT00940000160554; -.
DR   OMA; RVATIYI; -.
DR   OrthoDB; 4259465at2759; -.
DR   Proteomes; UP000264800; 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:SF119; PROTOCADHERIN ALPHA-C2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        19..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        695..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..138
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          139..247
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          248..355
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          356..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          582..680
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          736..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          954..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        957..974
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1000 AA;  108489 MW;  38E81F49020D53D1 CRC64;
     MAVTGKICNR TGSSINVPFY FVLFSLFCGL ACGQLRYSIT EELENGALVG DLAHDLGLDI
     RKLASRRIKI TSSSSGKRYL IVNPKNGKLL VNDRIDREAL CDLSSTCLIN LEVLVENPTE
     VHHVEVEIVD ANDNAPQFPR DEYQLEIIES ALPGSRYPIE NALDPDVGSN SVRMYQLSTN
     ENFALVSNKP SLNTKHIELV LKKPLDREQT PYHQLILSAV DGGIPDKTGT AKINIRVLDS
     NDNIPQFDSS VYKVKLLENS PKDTLVIKLN ATDLDEGTNA EVYYSFSSYT PERVRQMFSM
     DTNTGEIRVR SNVDYEETVS YEMYIQAMDK GPGAVAAHCK VVVEVVDVND NVPQIVLSSL
     SSPVREDARA DTVVALISVT DRDSGANKQV SLEIPAGLPF KIKSFRNYYT LVTSAFLDRE
     TTDAYNVTLS ATDGGNPPLS SQKTIQVDVA DVNDNPPRFE QTSYTVYVAE NNAPRASLCT
     VKAQDADIKE NARITYTVLN DNNHGIPVTS YVSVKADTGE AYALRAFDYE SLREFHFQVK
     AQDGGIPPLS RVATVYIYIM DQNDHAPVIV SPAGNGTRSL ETVQKNADSG ALVTKVVAYD
     ADAGPNAWMA YVLETATDLD LFKVHEHTGE IRTTRRILED NSTSFALTVV VKDHGQPALS
     STATINVAVM EIPPKVAPDT KKVSRPHNTL FLSNVTLYLI VALSATTFVF LVTVVVLAIV
     RCHAYCSQPG SCCGSQKPPP DGGSSSVSAG GGGSGGAAGQ PNNNVVLRRD LKVEPHYIEV
     RGNGSLTKTY CYKTCLTATS GSDTFMFYNT GRPISGTWGS GADRFFTSGS GFVRRLSMPD
     ASLQICPEPK APNADWRYSA SLRAGVQGAV HMEESSVVQG AQGMLVQNWP TVSSAADGEG
     GGELSPPVGA GVNSNSWHFR YGAGQGYMPP QPLKPGEIPP EAFIIPGSPA IISIRHDSGP
     VDDKGDFISF GKKEEAKKKK KKKKDKKDKK EKGKDDGGDD
//
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