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Database: UniProt
Entry: A0A182RM65_ANOFN
LinkDB: A0A182RM65_ANOFN
Original site: A0A182RM65_ANOFN 
ID   A0A182RM65_ANOFN        Unreviewed;      1186 AA.
AC   A0A182RM65;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 2.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:AFUN007337-PA};
OS   Anopheles funestus (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN007337-PA, ECO:0000313|Proteomes:UP000075900};
RN   [1] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA   Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA   Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA   Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT   "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT   Middle East: occurrence data, distribution maps and bionomic precis.";
RL   Parasit. Vectors 3:117-117(2010).
RN   [2] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA   Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA   Besansky N.J.;
RT   "A chromosome-scale assembly of the major African malaria vector Anopheles
RT   funestus.";
RL   Gigascience 8:0-0(2019).
RN   [3] {ECO:0000313|EnsemblMetazoa:AFUN007337-PA}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN007337-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC       {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
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DR   AlphaFoldDB; A0A182RM65; -.
DR   STRING; 62324.A0A182RM65; -.
DR   EnsemblMetazoa; AFUN007337-RA; AFUN007337-PA; AFUN007337.
DR   VEuPathDB; VectorBase:AFUN007337; -.
DR   VEuPathDB; VectorBase:AFUN2_012734; -.
DR   OrthoDB; 3816176at2759; -.
DR   Proteomes; UP000075900; Unassembled WGS sequence.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0048468; P:cell development; IEA:UniProt.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:UniProt.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR   Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR048286; Integrin_alpha_Ig-like_3.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF122; INTEGRIN ALPHA-PS1; 1.
DR   Pfam; PF01839; FG-GAP; 3.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF20806; Integrin_A_Ig_3; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 3.
DR   PROSITE; PS51470; FG_GAP; 4.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   ECO:0000256|RuleBase:RU003762};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003762};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003762}.
FT   TRANSMEM        1106..1130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   REPEAT          29..95
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          323..382
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          383..440
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          445..508
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          493..686
FT                   /note="Integrin alpha first immunoglubulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF08441"
FT   DOMAIN          687..838
FT                   /note="Integrin alpha second immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20805"
FT   DOMAIN          847..1095
FT                   /note="Integrin alpha third immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20806"
FT   REGION          102..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1144..1186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1144..1161
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1186 AA;  128479 MW;  DBE572426747C744 CRC64;
     MAHLDVLGAM VASLVLLMFS SVTTFNLETR HLLDKRGLPG SYFGYSVAGH SQRRAAGNTT
     TWMLVGAPLG QNLQPGSNHS GALYRCPITL ASNDCTQVIT DGHRTDDIDD EDGTGDSDNL
     HEHRLEPPGK DEIKNNQWLG VTVETGGQEN KIFVCAHRYI KINNPQSLAY AASGPGSTGL
     YLGQGVCYVL NEDFSFGFAV EVCRGRSIER EHQQYAFCQS GTSGAVLPDG TALIGTPGAM
     TWKGTLFNVA IEGGFLSRDK FQYFAPHDNL HSPVPNYSYL GMSVTGGRFF GEYMAYAGGA
     PRAAQGNGEV VIFANRYKKN PFDHVVSLRG EQFGSGFGST LASADINGDG RLDLLVGAPN
     YFNRTDGGAV YVYLNRGSSF VQQYDQRLTG RLESRFGTAI ANCGDLNHDG LDDIAIGAPY
     EASGTGRVYI HFGTKDGALS PEPVQTIDPT ELFANGGRTF GSSLAGGHDL DGNSYPDLIV
     GSYASDRVNA LFARPIINIR TYEEQQPIEP SSIDPTRIGC TSDPTANVTC FTFQACSAVD
     DASLNDGDVM ADSTLQLRCT IQAETFLKER KFSRVYFGTG VTPPGGNETG SNAASLSRTN
     ILRRRFRLAV NGKPVCHEVT AYLKEGTRDI QNPIQFRISY TLDEEREHGR GGGRARSRME
     RDLPRLEPIL NRTAAERTFT MPFQKDCGTD GICRSALAIH SAAVVGLTRG QSGSEAGNDY
     QLVVGLDRTL TLALTVQNKA DSAYETHLYV VHDSSLTYAG SKGSSVCGAH NATVVDCSIG
     NPLKRNGEVQ LSLRFDARSL EEYGYSNGPN GITHTVGMAV FVNTTSQDTG SKTRTALNLH
     IQRVAKVSMS GKALPEQVFY GSGDAQVMGE SAIHSLDEIG MSVEHKYQAS IYNDGPWRAP
     YVRLEIDWPL QVANNKPQGK WLLYLDALPM LDMSGIMGDG RSPCEVLPKN EPDGAVVPSN
     AASLVNPLGL PDGAGSTARS QMRSNYTQMR AQRMRRDRAM VLRPQTTDGA VQMDCASQTA
     KCVRIVCKIH DLGPKAHALV TVTARLWNAT LVGDYAHVDL VRIGSNARFT VEGLDELVDQ
     SQHPTSLTVR TEAFPEMGPP IVAMNVPWWI ILLAAIAGLL VLIAVTYILY RCGFFRRKRH
     TGEDPTLSGN LERRRDPTGG AYDELNDTNG SGGGTAERKP FLGRRS
//
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