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Database: UniProt
Entry: E9GGH2_DAPPU
LinkDB: E9GGH2_DAPPU
Original site: E9GGH2_DAPPU 
ID   E9GGH2_DAPPU            Unreviewed;      1021 AA.
AC   E9GGH2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Integrin alpha second immunoglobulin-like domain-containing protein {ECO:0000259|Pfam:PF20805};
GN   ORFNames=DAPPUDRAFT_303480 {ECO:0000313|EMBL:EFX81499.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX81499.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX81499.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(2011).
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU003762}.
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DR   EMBL; GL732543; EFX81499.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9GGH2; -.
DR   STRING; 6669.E9GGH2; -.
DR   EnsemblMetazoa; EFX81499; EFX81499; DAPPUDRAFT_303480.
DR   KEGG; dpx:DAPPUDRAFT_303480; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   HOGENOM; CLU_004111_5_0_1; -.
DR   InParanoid; E9GGH2; -.
DR   OMA; VEANFIS; -.
DR   PhylomeDB; E9GGH2; -.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0009897; C:external side of plasma membrane; 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:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; 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; 1.20.5.930; 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   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; 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:SF83; INTEGRIN ALPHA-PS3-RELATED; 1.
DR   Pfam; PF01839; FG-GAP; 2.
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; 3.
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   Reference proteome {ECO:0000313|Proteomes:UP000000305};
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        42..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   TRANSMEM        958..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   REPEAT          69..138
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          368..431
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          433..491
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          585..688
FT                   /note="Integrin alpha second immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20805"
FT   REGION          996..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1021
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1021 AA;  112655 MW;  684A593B2C1C302D CRC64;
     MAGFQEKRKK NYSAFTKGRK RCVSGATLGD FNSGSCKFSA RLFLWVMVCF VVGLVSSFNI
     DTVHPLVYED PAAGQNARES YFGYSLQFLF NQKDNAHNSA KWLLVGAPRA NSTFPSHANL
     KEPGQVYRCL LGNPNRDQCQ PLIVESEASQ FNRDRLYKDR KDYGWLGGAM AVNNPSTGRV
     AVCGYRWSNS LSSTEHYMNG ACYWNNHQVS ENKDFVKVLP IVSKEQQVIG NDRNGTYNYA
     YGQSGFSVHM ALKKDKIEEM IIGAPGVFKW TGAVIRVSDY SPDNPSGVPS RRKRQDTQDI
     IEFGDTLVTN SAKISVLEPN DYFGYSVHSG IFFNDGKLLY VSGAPRAAGM KGKVLLFDFF
     PGQDSQLNIR LELNGTQLGE YFGASVLAVD LTGDGKAELL VGAPQHSLQP ELGDRTGDEG
     KVYFYLNRND NLERSPALFG SKAKDARFGT TMASVGDINR DGFNDVVIGA PYENDKGAVY
     IYLGGMYDIH RHPETGYWQR IAAADFVFPL NNLKGFGISL VAADMDGNSY PGVGYNFHFD
     AEYVNQPRLI LDIDEMKDTF CATCPVIDKT EKNYIEESAA FTSECGADNI CKEDLEVEAN
     FISNLKELVI GSKSTISFEV KLVNHGEPSY LTTLDIQLPS YTNLKRTPAD LCQKPSFASS
     EELIYSCQLR VNPLKRAKTE RMEFELDLMS VPSGGSDVLT VVVEARMNGV AAMGRQPLFN
     LTMPLRTAID VEILGNSVEE QQTYQRSNET KVSAGLKDRI IFKHLYEVRN VLPSAAEVEI
     EILIPNSVFS TQGVTLPVVE LPSISIDATQ KGGLSNTVCR LDYNSGQSID DIQRFREFIN
     SSPTVKIQPP FKFGLVANRT AFIDCFNTPN ANCVKYICSA FGPLSTESPI RISLTGTLLL
     QNIFSFMVNE DVFILSSAAR VVIRQPANNV PQPYGHKPDV AIATTYFLPQ GPPGTLAVAS
     WIIVLAVLAG IILLSLMVVG LHKMGFFKRQ RYPQDGGLME ETTTPGDGNS EGTDTEPQPN
     A
//
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