ID W5J2Y7_ANODA Unreviewed; 1015 AA.
AC W5J2Y7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Fermitin 1 {ECO:0000313|EMBL:ETN58682.1};
GN ORFNames=AND_009668 {ECO:0000313|EMBL:ETN58682.1};
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:ETN58682.1};
RN [1] {ECO:0000313|EMBL:ETN58682.1}
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:ETN58682.1}
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:ETN58682.1}
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).
CC -!- SIMILARITY: Belongs to the kindlin family.
CC {ECO:0000256|ARBA:ARBA00008052}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETN58682.1}.
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DR EMBL; ADMH02002125; ETN58682.1; -; Genomic_DNA.
DR AlphaFoldDB; W5J2Y7; -.
DR STRING; 43151.W5J2Y7; -.
DR VEuPathDB; VectorBase:ADAC009668; -.
DR VEuPathDB; VectorBase:ADAR2_005475; -.
DR eggNOG; KOG3727; Eukaryota.
DR HOGENOM; CLU_011611_0_0_1; -.
DR InParanoid; W5J2Y7; -.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13205; FERM_C_fermitin; 1.
DR CDD; cd17096; FERM_F1_kindlins; 1.
DR CDD; cd01237; PH_fermitin; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR037843; Kindlin/fermitin.
DR InterPro; IPR040790; Kindlin_2_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037837; PH_Kindlin/fermitin.
DR PANTHER; PTHR16160; FERMITIN 2-RELATED; 1.
DR PANTHER; PTHR16160:SF13; FERMITIN 2-RELATED; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF18124; Kindlin_2_N; 2.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889}.
FT DOMAIN 708..815
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 62..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 114210 MW; 65B421A11F2F92EA CRC64;
MIHVGDNTWN LKVFITDLQV TKTLRVRGDL HIGGVMLRLV DPGKAAIARR CMGPAAAAGQ
ARLVESSQQP APPAPRSPPG GTYHHRSIHG EKADLSVVLL GLLRRWLALM LLRFCFGDCR
RRYVIIAIVA SHQHQNQHQH INHTAASAAS GAGSGGKRTA HQDELREFPI SECSIDAKDA
KEKGSYPAPR PGCADENPKD WSDHALWWPV RNQWLTRTKS TLDQVGLHAD ALLHFTPMHK
TLRVQATQSN GICQRKLRAK LHAITANYLR EHSGHTTSAD VRCCGQCRPV MVVVTCDSWR
YCCERANDRS DPPQIETRSD TQSDPILKPN DAIAGRWKCQ TTPRTTIPEH PHLSGLTNSG
GDHIRTLSSV WILDDKLIRH DPLRKETEEE KEERGHMPDL RYLDCRVDFS IKTFGAVVAL
CKDLGIRHPE ELSLCKPLEP MHLKKNYADL AKKKIPIEHN GSGRDYIQPA VDTNTFIPVT
AHNLNGSNGS LDGPMNHGPF SCAPVPHSNS FSTPKQGLQS TPISSPTGTL RHGHASSGFS
ESSSSIGDPA DNLAYSPCAP SPEARSRLVK PKTLIERARM NIGWLDSSLS IMEQGIREFE
TLCLRFKYYT FFDLNPKYDQ VRINQLYEQA KWQLLNEEID CTEEEMLMFG ALQLQVNLQN
EIPQPDSGID TSSLDNAADD DVDAALRELQ ITLEGPSNGV NAGDITHIPE LTDYLRFLKP
KKFTLKGYKR YWFTYKDLHL HLYKSREDAR ANNAPQVTIN LRGCEVTPEV NLSQKKFNIK
LEVPLEQSIN SEMWIRCDNE EQYAKWMAAC RLASKGRSLA DSSYDSEVAS IRSFLSMQKP
AQAPAININP SAMDPNEYLA PRYSKKLKSK GIMRMLEAHA NVKDLPLIEA KLSYIRAWQS
LPEFGVTLFV IKFDGHKKEE LLGVASNRIM KMDITTGDHL KTWRYNTMKA WNVNWEIRCM
MVQFQGESVV FSCLSADCKV IHEFIGGYIF MSMRSKETNQ TLNEELYHKL TGGWN
//