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Database: UniProt
Entry: A0A2K5CTT9_AOTNA
LinkDB: A0A2K5CTT9_AOTNA
Original site: A0A2K5CTT9_AOTNA 
ID   A0A2K5CTT9_AOTNA        Unreviewed;      1339 AA.
AC   A0A2K5CTT9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Cadherin domain-containing protein {ECO:0000259|PROSITE:PS50268};
OS   Aotus nancymaae (Ma's night monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000012102.1, ECO:0000313|Proteomes:UP000233020};
RN   [1] {ECO:0000313|Ensembl:ENSANAP00000012102.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein.
CC       {ECO:0000256|ARBA:ARBA00037723}.
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DR   Ensembl; ENSANAT00000029920.1; ENSANAP00000012102.1; ENSANAG00000023977.1.
DR   GeneTree; ENSGT00940000158335; -.
DR   Proteomes; UP000233020; 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:SF254; PROTOCADHERIN-11 X-LINKED-RELATED; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1339
FT                   /note="Cadherin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014416545"
FT   DOMAIN          53..139
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          140..249
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          250..355
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          362..466
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          467..570
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          571..673
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          685..795
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          920..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1056..1116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1317..1339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1102..1116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1339 AA;  146279 MW;  7CC9687B86DC9BF5 CRC64;
     MDLLSGTYIF AVLLACVVFQ SGAQEKNYTI REEMPENVLV GDLLKDLNLS RIPDKSLKSP
     MQFKLVYKTG DVPLVRIEED TGEIFTTGAR IDREKLCAGI STDTQCFYEV EVAVLPDEIF
     RLVKIRFLIE DINDNAPLFP TTVINISIPE HSAINSIYVL PAAIDPDVGI NGVQNYHLIT
     SQNVFGLNVT ETPEGDKMPQ LIVQKELDRE EKDTYVMKVK VEDGGSPQRS STAILQVSVT
     DINDNHPVFK EEEIEVSIPE NAPVGTSVTQ LHATDADIGE NARIHFYFSN LVSNTAKRLF
     HLNATTGLIT IKEPLDREES PSHKLLVLAS DGGSTPAKAM VLVNVTDVND NVPSIDIRYI
     INPTNGTVVL SENAPLNTKI ALITVTDKDA DHNGRVTCFT ELDIPFRLRP VFSNQFLLET
     ASFLDYESTK EYAIKLQATD AGQPPLNESS MLFIKLKDEN DNAPVFTQSF VSLSVPENNF
     PGIQLTKVSA KDADSGPNGE ISYLLGTDAP PEFDLDPRTG MLTAVKKLDR EKQETYLFTV
     LAKDNGEPPL TSNVSVFLSV IDQNDNSPVF THNEYNFYVP ESLAKHGTVG LITVSDPDYG
     ENSAVTLSIV DMNDYFTIDS ETGVIQPNIS FDREKQESYT FYVKAEDGGR VSRSSSAKVT
     INVVDVNDNK PVFIVPPSNY SYELVLPSTN PDTEVFKVIA VDNDTGMNAE LRYSIVGGNT
     KDLFEIDEVT GNITLKEKCV VTDLGLHRLL VKAQDLGQPD SLFSVVIVNL FVNESVTNAT
     LINELVHKNI ESPVTQNIEI ADTSSPISDY VKILVAILSG IITVIVAIFI AAVVRCHQAP
     HLKAAQKNKQ NSEWATPNPE NRQMIMMKKK KKKKKHSPKN LMLKCVTIEE TKTDDVDNDG
     NSVTLDLPID LEEQTMGKYS WSTTPTTFKP DSPDLARHYR SSSPQPAFQI QPETPLNSKH
     HIIQELPLDN TFVACDSISK CSSSSSDAYS VSDCNYPVTT FEAPVSVHAR PPMKDIVISG
     TTMKESTTVE IWIHPQLQRK PEGKGAAKSQ RRVTFHLPEG SQENSSDGGL GDHDAGSLQG
     TSHALPLGYP QEEYFDHATP NNRTEGDGNS DPESTAEITV QPTVEEASDT CTQECLILGH
     SDACWMPASL THSSSSQAQA SALCHSPPLS QASTPDHSPP VTQTVALCHS PPVTQTVALC
     HSPPPIQASA LRHSRPLVQV TALCHSPPSA QASVLCYSPP LAQAAAICHS SPLPQVTALH
     LSQAQTSVSL QQGRVQGADG LCSVDQGVQG SATSQFYTMS ERLHPSDDSI KVIPLTTFTP
     GQQARPSSPD SPIMEEHPL
//
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