ID W5JRM3_ANODA Unreviewed; 1976 AA.
AC W5JRM3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Cadherin {ECO:0000313|EMBL:ETN65565.1};
GN ORFNames=AND_002658 {ECO:0000313|EMBL:ETN65565.1};
OS Anopheles darlingi (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN65565.1};
RN [1] {ECO:0000313|EMBL:ETN65565.1, ECO:0000313|Proteomes:UP000000673}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT the genome of the newly sequenced Anopheles darlingi.";
RL BMC Genomics 11:529-529(2010).
RN [2] {ECO:0000313|EMBL:ETN65565.1}
RP NUCLEOTIDE SEQUENCE.
RA Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETN65565.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23761445;
RA Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA Camargo E.P., de Vasconcelos A.T.;
RT "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL Nucleic Acids Res. 41:7387-7400(2013).
RN [4] {ECO:0000313|EnsemblMetazoa:ADAC002658-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; ADMH02000623; ETN65565.1; -; Genomic_DNA.
DR STRING; 43151.W5JRM3; -.
DR EnsemblMetazoa; ADAC002658-RA; ADAC002658-PA; ADAC002658.
DR VEuPathDB; VectorBase:ADAC002658; -.
DR VEuPathDB; VectorBase:ADAR2_001930; -.
DR VEuPathDB; VectorBase:ADAR2_008275; -.
DR eggNOG; KOG0061; Eukaryota.
DR eggNOG; KOG3594; Eukaryota.
DR HOGENOM; CLU_234338_0_0_1; -.
DR OrthoDB; 2907364at2759; -.
DR Proteomes; UP000000673; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:UniProt.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:UniProt.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 5.
DR CDD; cd00053; EGF; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.60; Cadherins; 5.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF422; NEURAL-CADHERIN 2-RELATED; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF00028; Cadherin; 3.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00112; CA; 5.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000673};
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 335..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..267
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 579..716
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 717..828
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 829..947
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 948..1052
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1052..1171
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1428..1464
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1465..1671
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1674..1714
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1717..1908
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DISULFID 1454..1463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1704..1713
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1976 AA; 220301 MW; FE289F9C68A3B41F CRC64;
MAINFHFDNV VYRARDSASG DRGDPAAAGP LPLLGGLSGQ FTGGRLTCLL GPSGAGKTTL
IDVLSGYRER GLASGTFQLT GRGPGTLDST ADSLTATTRR QLIGYCRQDE SLFPELTVTE
TLRYAAAFRQ SPAVRNGHRT VEDTLRLLAL DGPTVRDARV AVLSGGERKR LAIGLELVGE
RRILFLDEPT TGLDSCTALA ILKHLRELAG GDPACPRIVL CVIHQPNSAL FRLFEEVFVL
RRGRFLYRGP IGAPLERTLD QAGVQHCPLS YNPADYVLEL ACREETDPAV QYLLEQFASP
SRRPTPVPVP FLSSPETPTP NGTVDGNRRM SIALLLGRVL FQIVGSVLFG LLMYGVANDA
EKTMQSVSSV FVQLVMVWIA NATTTVTVTV AELPIAGKEY ARGWYSTGAY FLSLVAFQLP
ITALGSVPAA IILYLLTTGG GGAAGVLEDT SGPDRLAMHV LIMFLTACIG QSVGMLLGAL
FRLETAILMV PYANITFFFV NSYFVRVRDA LPVVQAVARL SYFQYSFEGA ISALYGYGRP
DLPCDELFCY FRKPRKVLHV LDVAGDRFAL DALVLGLWIG ALNVTATDGD KDRPQNIVYF
LTGQGIDPDN PANSKFDINR TTGEIFVLKL MPPRRSLGSS VSSGSSSSSL SYLKLHQQQQ
QQQQQQCLSP LDRDQPNGRP QWRFTVFAQD EGGEGLVGYA DVQVNLKDIN DNAPIFPQGV
YFGNVTENGT AGMVVMTMTA VDYDDPNEGT NAKLIYSIEK NVIEEETGSP IFEIEADTGV
IKTAVCCLDR ERTPDYSIQV VAMDGGGLKG TGTASIRVKD INDMPPQFTK DEWFTEVDET
DGTNLPEMPI LTVTVHDEDE TNKFQYKVID NSGYGADKFT MVRNNDGTGS LKIVQPLDYE
DPLQSNGFRF RIQVNDKGED NDNDKYHVAY SWVVVKLRDI NDNKPQFERP NIEVSVYENA
DVGKTLETFK ATDPDQGGKS KVSYAIDRSS DRQRQFSINQ EGTVTIQRNL DREVTPRHQV
KILAIDDGIP PKTATATLTV IVQDINDNPP KFLKDYRPVL PEHVPPRKVV EILATDDDDR
SKSNGPPFQF RLDPGADDII RASFKVEQDQ KGANGDGMAI VSSLRSFDRE QQKEYLIPIV
IKDHGNPAMT GTSTLTVVIG DVNDNKMQPG SKDIFVYNYL GQAPDTQIGR VYVYDLDDWD
LPDKKFHWET QEHPRFKLDE DTGMITMRQG TRDGRYHLRF KVYDRKHTQA DVPANVTVTV
REIPHEAVVN SGSIRIAGIT DEDFIRVWNY RTQSLSRSKS DRFKDKLADL LNIDRENVDV
FSVQLRRKHP PLTDVRFSAH GSPYYKPVRL NGIVLMNRED IEKEVGINIT MVGIDECLYE
NQMCEGSCTN TLDINSLPYM VNANKTSLVG VRVDVIAECT CGARNFSKAE SCRSSPCHNG
GRCMETRYGL SCSCPTGYTG PRCQQTTRSF RGNGWAWYPP LDMCDDSHLS FEFITRKSDG
LLLYNGPIVP PERDELLVSD FISVELERGF PRLLIDFGSG TLELRVKTKK SLDDGEWHRL
DVFWDTENVR MVVDNCRSAE VSEMEDGSPP EFDDSSCQAR GTIPPFNEYL NVNAPLQIGG
FYREQFDPTH YRWNYMPMGK GFDGCIKNLV HNSKLYDLAH PGLSRNSVAG CPQTEEVCSQ
SEQTSRCWEH GNCVGSFTEA RCQCRPGWTG PACNIPTIPT TFKQQSYVKY ALSFEPDRFS
TQIQLRFRTR EQHGELFRVS DQHNREYGIL EIKDARLRFR YNLNSLRTEE KDIWLNAIAV
DDGQWHVVRV NRHGSAATLE LDGGEGRRYN ETFTFEGHQW LLVDKQEGVY AGGKAEYTGV
RTFEVYADYQ KSCLDDIRLE GKHLPLPPAM NGTQWGQATM ARNLERNCPS NKPCANVICP
DPFECVDLWN EYECTPDPSV RSVHESVQTP ASILFNIFQT NLDDISGQPV ITDGDD
//
