ID   Q1G0S7_MANSE            Unreviewed;       952 AA.
AC   Q1G0S7;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Hemocyte-specific integrin alpha subunit 1 {ECO:0000313|EMBL:ABF59518.1};
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130 {ECO:0000313|EMBL:ABF59518.1};
RN   [1] {ECO:0000313|EMBL:ABF59518.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17553801; DOI=10.1074/jbc.M700341200;
RA   Zhuang S., Kelo L., Nardi J.B., Kanost M.R.;
RT   "An integrin-tetraspanin interaction required for cellular innate immune
RT   responses of an insect, Manduca sexta.";
RL   J. Biol. Chem. 282:22563-22572(2007).
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   EMBL; DQ531844; ABF59518.1; -; mRNA.
DR   AlphaFoldDB; Q1G0S7; -.
DR   EnsemblMetazoa; XM_030168362.2; XP_030024222.2; LOC115443096.
DR   OrthoDB; 3214447at2759; -.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
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; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
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; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 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; 1.
DR   PROSITE; PS51470; FG_GAP; 2.
PE   2: Evidence at transcript level;
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, ECO:0000256|RuleBase:RU003762};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003762};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003762}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   CHAIN           19..952
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT                   /id="PRO_5001425750"
FT   TRANSMEM        861..884
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   REPEAT          253..314
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          318..376
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          572..682
FT                   /note="Integrin alpha second immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20805"
SQ   SEQUENCE   952 AA;  106359 MW;  673045B460B53E47 CRC64;
     MMLLWLLLMA QLAWPTSALY HEKSLKVFQP GDLKSPLRKE ANFGFSIAYQ SATQSLIISA
     PTADYIGRIY SCDIELKRNC TVVPYDIKRD DPLYNHDYWL GATVKAGPDY FVTCAPRYVE
     VGSSYNLPGE FSHCYRSSKH SKLLPISQIS SQQRRVNTKK FEDEMDSFGW SMDLKDRKIL
     FGGPAMFSGR AMASADSAIT SISGHSKGVD VKYNLGYSVA IGAFFSDKIV YAVGSPFGQN
     GRGKVVFFNK DWKVMSSISH KNIGTMFGAV LATAHIFSDS LTDLLVGAPT EAANHDYDTG
     AVYYYKTGSR RSVQMSIEHT KIISGYQPGS LFGSAIISVG DLNGDGKDEI AIAAPYEDEG
     KGAVYLYCGS SFLDASSNVL LQRLQPEGLH TFGLSLSSPS DYDENGCNEL AIGAPQDNAV
     VLYKCLASVV LTVFAVFPNL RDRRNVKSPY PDRNETYFVF DSCFDVKYPK KLKTVIAKIE
     VTVQIKHPDA TLAMPHKDGK YNVTLDIKKT RYCEKIGVST PEHGNYNIKI FYNIQARLVN
     SPINETDFDG KRVILSGRSE LSISDNVWAA ECKVQNACKA DLSLKIATSP RGSYMIGSME
     PIKVNMILEN KGEIAYDACV ELQLEGAAMK KTPTTSCTHH PLTNTLKCAP SYALKTDKSW
     ETTDIILKTE TLTNKNKQIN LTSRLYEHCT DPATFKEQNY TITVLANSEG ITVNGKTNIG
     DVVSMTTLEV TDSGKQFQHN YMIQNDGITW EDVTCEIILP KLPYVNYPQK AVTVFIQQNS
     FECNMTDDLS PDYITANCKL SSIKQNIITF IIVLIQVPPT TLDDILYKQN VTIKSTLKLH
     FDDGDKTYSV ATEVMLRDTG IPWWIILLAA LIGLLILIIL ILILRQYGFL KRKERKKLQE
     LRKSVRRQTV RRSMMQQQVE DRQRLTDVPI EATETDVPCG IEPDHRVEVN IK
//