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Database: UniProt
Entry: G1KCB0_ANOCA
LinkDB: G1KCB0_ANOCA
Original site: G1KCB0_ANOCA 
ID   G1KCB0_ANOCA            Unreviewed;      2548 AA.
AC   G1KCB0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=Neural-cadherin {ECO:0008006|Google:ProtNLM};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000003770.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000003770.3, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000003770.3,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000003770.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC       {ECO:0000256|RuleBase:RU004357}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC       ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   STRING; 28377.ENSACAP00000003770; -.
DR   Ensembl; ENSACAT00000003862.3; ENSACAP00000003770.3; ENSACAG00000003855.3.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000164400; -.
DR   HOGENOM; CLU_000347_1_0_1; -.
DR   InParanoid; G1KCB0; -.
DR   TreeFam; TF351842; -.
DR   Proteomes; UP000001646; Chromosome 4.
DR   Bgee; ENSACAG00000003855; Expressed in embryonic post-anal tail and 2 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   CDD; cd11304; Cadherin_repeat; 13.
DR   CDD; cd00054; EGF_CA; 4.
DR   CDD; cd00110; LamG; 2.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.60.40.60; Cadherins; 14.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF442; DACHSOUS CADHERIN-RELATED 2; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 12.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 13.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF49313; Cadherin-like; 15.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00232; CADHERIN_1; 6.
DR   PROSITE; PS50268; CADHERIN_2; 14.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00043};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   ECO:0000256|RuleBase:RU003318};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003318};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2352..2372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..174
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          175..275
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          285..377
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          378..484
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          496..593
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          594..693
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          694..805
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          806..920
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          921..1022
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1023..1129
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1140..1243
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1244..1351
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1361..1457
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1457..1571
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          1821..1860
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1861..2038
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2034..2073
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2076..2253
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2254..2290
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2298..2335
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1850..1859
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2063..2072
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2325..2334
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   2548 AA;  281476 MW;  AC3140F39C1B9BBF CRC64;
     MPALRLRNGD EHQPPESDMT GLNVRGKPLP LPFFQSHSPV LKLPYMLALL SESDWYICRV
     VVIAVEEEPI SWGMFPYPYL ARIDPEARAG TLVYQLAAHY SNNENSSTGI SYALIAGGEE
     RFDIDTDTGA LLTTGLPLTL NQEYVVTVLA IDEYGSKSPY AFISILAGSR PPQFTNMSYS
     VFIPENTPPN ERVADVEAVS FQSQPICYTL LMNPSGLFIL DQETGELSLT HAVDYESEHH
     LYHFLVKAME RESLLSSVTE VIVHITDEND CFPEFQQSIY SRENILESIP IGTSLLQVLA
     TDCDSGSNSE IIYFLQTADF SITPEGVISS NQQLDFEQSN HMYEFVVIAV DQGHPARTGT
     ASVRIRMANV NDESPVFSQS VYETFLSEDA GPGTLVATIL AKDPDGDGVM YLISGGNEEG
     NFELDSRKGI LRLRRNPVPK LKGPEYVLNI SAIDDNTSGG PRSLCSFAEV VVGINDINNN
     KPIFRECAYY SDNTWVLENQ PPGTYVLRVE AYDADLGQNG EVKYSLMHRD GSLPGFSIDP
     DSGVITTTRS FDREKQREYM LSVIATDQAQ EPLIGMCQIT IYIADENDND PKFENSRYQY
     FLREDTPVGT SFLCATAHDD DQGANAAITY SMVQQEPEYF KINPSTGWVY VNHVISQTFQ
     INRYITATDG GNRSSTVELT VTITDVLNQS PQWDESSYSI TIPESTARDT KIVTVKATSP
     LGDPRVTYHL EEGQVPETNM PVRFYLKPNR ADGSASLLVA EPLDFETTKL FTLSIKAQNV
     ATIPLASFTT VYVNITDVND NVPFFTSSTY EVSVPEGAGI GTSVMQVLAT DADSGLNGEV
     HYSILKDSSG DYQYFTIDST SGVISTLASF DREKRASYLI EVQSQDSSES ARPGIYGQPN
     TDTAYVRIFI SDVNDNCPAF PHLVYETDVD EDQDVGYAVL TATATDKDEG SNAKLRYQIT
     SGNEQGDFYV EPEKGTILIA QHLDYEQERH YKLQLVTSDG KWENHTLVVI NVININDEAP
     VFSQDEYHGS VLEELADLPV LVLQVSATDP DQETKQGGFC YSLHGQGAQS EFSINELTGE
     ITANERLDRE KRSMWRFLVL ATDEDGEGLT GFADVIIEVL DVNDNAPLFL CASDGCFMGQ
     IPEDSPADST VMEMLAIDLD DPAAGKNAVL TYNIIQNVKN EINLNLFSVN PVTGTIYTVL
     STLDREKRDK YLVVVEAKDG GGLTGTGTAT ILVTDINDHA PAFTQKIYTA FVSEGASVNT
     LVAEVSATDE DEGENAVVTF SILDGDDDHK FYIETDKANK CGVIRLRKEI DFEKPHERVF
     NLTVKAEDLD FFSIAHCVIY VEDYNDHAPL FYPQFYEVAG LAEDVSLGTK VVQVIGIDLD
     SGLNGRFSYR LLNKSDPSGR FSVANDGWVI VAGELDYETV AQYQLVVIAT DMGQPALSSS
     ATVLVALQDV NDNGPEFDAL YNPVVWENTP SPQVVQMNDT STLLYAKDRD SPANGAPFSF
     HLLSDFGSVT YFNLQDFSNG SAMLIALHTF DREVHKVFHL RILIADSGNP PMSSTNTLTV
     NIGDRNDHPH AAGYMECLIY SYNGILPTTV LGKIHAPDND DWDHKTYHFE EKAPRHFILN
     DNSGLLSIKE GTPAGIYDLR VKVTDGIWPD VVSTVKVVVK EIKEEAAHNA GSVRIRDITA
     EDFIYQSSES ESKYNQMKML FSEIISAQLE NVHIFSVLNS PGETQGVDIW FAIHGSPYYK
     AEKLNGNIAV SKARLETVLN INITQIGIDE CVTANCSHST GCISKNEFSP LPTITTSGNV
     LLASVTVFSN AQCTCEARER KHHSCSSYRI NPCFNGGTCT DTDLGYSCKC PNTFHGPECQ
     QTQHTFRGHG YAWFPPIKPC FQSRISLDFI TEVADGLLLY NGPVARVKPG EPSFAGLKWR
     HTKLSSHKCR KVQLILDHCA NVSFTNNDDA QEDVSKVDHS VCKVSSETPG SDRNLDVHQP
     LQLGGVKKAQ PYHTSQKHFK GFVGCIRNVI IDSQVYNLEQ PAESLNSAPG CSLTDGLCQK
     SGIPSCGVHG KCIGDWGSFN CDCFTGYMGA RCDKALLEWN FGKDSWILYD LKNVFSAYNT
     HVRLSVRTRT SSSTLLSLAS SVGNGFIRLE IIGGYFGVSF NFGGKDHVLQ LSTVRIDNGQ
     WIELTLERYH NEFSLLINDG GGDHEVSAIL GSGGQFKINL ARIVLGNRLV NHSESDFQGC
     MRDVRLNGQP LLVNGESTEY SFIVEQEGIT IGCHSNSCSN QPCYNPFHCV DLWRKYECRC
     PAGKVEVTDN LTGLKQCTSS PCGHWNCRNG GTCVAQSRDK YVCQCPEGYK GKWCEVSPVK
     AGRPVGLSSG SILAISMCLL VFLGLLVSYT VWSQWGRSRF RKGGIYHIPE EHESWDDVRE
     NVFNYNEEGG GEHDLSAYNL DTLKKPVQII PPFSSGTAAP VLRSYSGSQI NPHGNPACLR
     ETPSLDTSLP DFKHCMSQRI QNADSNQKHL PTDSMHFYCL EGQGSPAGSL SSLETSSVEQ
     DLNYENLNEW GSEFVKLKQL HELRTEQL
//
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