ID Q7PME7_ANOGA Unreviewed; 803 AA.
AC Q7PME7;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 145.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=1279656 {ECO:0000313|EnsemblMetazoa:AGAP010233-PA};
GN ORFNames=AgaP_AGAP010233 {ECO:0000313|EMBL:EAA13939.2};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA13939.2};
RN [1] {ECO:0000313|EMBL:EAA13939.2, ECO:0000313|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13939.2,
RC ECO:0000313|Proteomes:UP000007062};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EAA13939.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13939.2};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAA13939.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13939.2};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EAA13939.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13939.2};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EAA13939.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA13939.2};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EnsemblMetazoa:AGAP010233-PA}
RP IDENTIFICATION.
RC STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP010233-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU000633};
CC Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000633}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR EMBL; AAAB01008980; EAA13939.2; -; Genomic_DNA.
DR RefSeq; XP_319420.1; XM_319420.2.
DR AlphaFoldDB; Q7PME7; -.
DR STRING; 7165.Q7PME7; -.
DR PaxDb; 7165-AGAP010233-PA; -.
DR EnsemblMetazoa; AGAP010233-RA; AGAP010233-PA; AGAP010233.
DR GeneID; 1279656; -.
DR KEGG; aga:AgaP_AGAP010233; -.
DR VEuPathDB; VectorBase:AGAP010233; -.
DR eggNOG; KOG1226; Eukaryota.
DR HOGENOM; CLU_011772_0_1_1; -.
DR InParanoid; Q7PME7; -.
DR OMA; KQGMGAC; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
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; IBA:GO_Central.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF59; INTEGRIN BETA-NU; 1.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU000633};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007062};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..803
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014587781"
FT TRANSMEM 731..753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..468
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 467..504
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 519..558
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 561..595
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 602..635
FT /note="EGF-like"
FT /evidence="ECO:0000259|SMART:SM00181"
FT DOMAIN 754..800
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 39..49
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 42..75
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 52..64
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 203..210
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 258..299
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 489..535
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 494..503
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 541..546
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 543..570
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 548..557
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 559..562
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 578..583
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 580..612
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 585..594
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 596..603
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 618..623
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 625..634
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 645..654
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 651..726
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 803 AA; 90927 MW; FF5BC3808787E688 CRC64;
MTAFKISVTL LVTTYLLSLA FGQSSRVVTQ SKCFFQKNCI ECLDADKDCA WCTDELYDMR
KSRCMTKHEL LESKCNALKI ETNDDYSFLQ IGKNEPHRDF DSQQLEAVQI MPQKMNLRLG
KLGSRTISFK YKPAKNYPLD MYYLMDLTWS MRDDKATLES MGSQLALALA NLTANYQLGF
GSFADKPAFP FIQSEPHRLQ NPCYSENDQC EPTYGFKHRL KITRDIDSFI AQVKESNVTG
NVDNLEAGLD ALMQVLVCEK QIGWGSNTRK IVIVATDGWL HMAGDGLLAG IVEENDKQCH
LDSDGNFVDA LKYDYPSLEQ IWRVLLRSKT AVIFAVTEAQ QAYYRRLSDL MPEFTSVGRL
QDDSSNIIQL VDEGYREFVK RVEFIDNSPD YMQLRYTTDC AGLYREPQPI NRCDNIEIGK
EYKFNVEIHL LEYPKDPSIT NVTVRIEEKL ISNEAVELDI DLRTSCNCEK NKKPMELSEL
CNFNGDYVCG QCQCYVGWIG KTCECNLQNS QNRRELFEQC VAPSVGDELR TGPICSDRGE
CICGQCYCNP GFEGEHCECN ECATIDGSIC GGPDHGICTC GTCSCFDSWS GDNCECTTDT
TGCKAPSNDA VCSGHGQCNC GRCSCDESFF GPFCETKDGE QPALCSSYED CIRCAVHEIN
NIPCQDLDNK CREKIGLYKV QLVDATDNSL NCTFRFSDEK NVCDYRFSYE LANNRETLLK
VQNLQCKEIN LIAAGFTIAA SIIIGGLLML FCYRCKIMYD DRKMFAKFEK EREQETKYQM
ESPLYKSPIS NFKVPAEMET SVL
//
