UniProt: A0A212FB66

Database: UniProt
Entry: A0A212FB66_DANPL

LinkDB:  A0A212FB66_DANPL 
Original site:  A0A212FB66_DANPL

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Ontology (3)   
   GO (3)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (23)   

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ID   A0A212FB66_DANPL        Unreviewed;       759 AA.
AC   A0A212FB66;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN   Name=LOC116779725 {ECO:0000313|RefSeq:XP_032530017.1};
GN   ORFNames=KGM_214289 {ECO:0000313|EMBL:OWR50970.1};
OS   Danaus plexippus plexippus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Nymphalidae; Danainae; Danaini; Danaina; Danaus; Danaus.
OX   NCBI_TaxID=278856 {ECO:0000313|EMBL:OWR50970.1, ECO:0000313|Proteomes:UP000007151};
RN   [1] {ECO:0000313|EMBL:OWR50970.1, ECO:0000313|Proteomes:UP000007151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR50970.1};
RX   PubMed=22118469; DOI=10.1016/j.cell.2011.09.052;
RA   Zhan S., Merlin C., Boore J.L., Reppert S.M.;
RT   "The monarch butterfly genome yields insights into long-distance
RT   migration.";
RL   Cell 147:1171-1185(2011).
RN   [2] {ECO:0000313|EMBL:OWR50970.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F-2 {ECO:0000313|EMBL:OWR50970.1};
RA   Zhan S., Reppert S.M.;
RT   "MonarchBase: the monarch butterfly genome database.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:XP_032530017.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) 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; AGBW02009374; OWR50970.1; -; Genomic_DNA.
DR   RefSeq; XP_032530017.1; XM_032674126.1.
DR   STRING; 278856.A0A212FB66; -.
DR   EnsemblMetazoa; XM_032674126.1; XP_032530017.1; LOC116779725.
DR   KEGG; dpl:KGM_214289; -.
DR   eggNOG; KOG1226; Eukaryota.
DR   OrthoDB; 5475862at2759; -.
DR   Proteomes; UP000007151; Unassembled WGS sequence.
DR   Proteomes; UP000596680; Chromosome 5.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
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; IPR013111; EGF_extracell.
DR   InterPro; IPR040622; I-EGF_1.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR   PANTHER; PTHR10082:SF60; INTEGRIN BETA-PS; 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   PIRSF; PIRSF002512; Integrin_B; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01241; Integrin_b_cyt; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF69179; Integrin domains; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS00243; INTEGRIN_BETA; 1.
DR   PROSITE; PS50234; VWFA; 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:UP000007151};
KW   Signal {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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..759
FT                   /note="Integrin beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041057979"
FT   TRANSMEM        691..713
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          127..324
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DISULFID        29..40
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        43..53
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        231..272
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        372..377
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        425..429
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        450..488
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        455..464
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        494..499
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        496..525
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        501..510
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        531..536
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        538..547
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        549..554
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        569..574
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        576..590
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        601..610
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ   SEQUENCE   759 AA;  85348 MW;  CC939C230EE1CFC2 CRC64;
     MHILYQISLV LCCFTLISCE SNCHNFDTCG GCIGYAFDRC VWCAAKNHSE RRCQSKSTLP
     ANATWCGEAV YDPEFNKNVI SNENFNTGQD GMKTVQFRPQ SIKIKARPGV PVDFMMSYKP
     ATDYPLDLYY LMDYSKTMQV HATTLMEQGY KIYKELRKLT NNVRLGIGSF IEKPALPYAD
     ISVAESYSFK NHLSLTDNMT LFERAINETL FGSNYDDPEA GFDALMQAMV CIKEIGWREN
     SRRIIVLSTD STYHSAGDGK FVGAVLKNDM QCHLDGNIYG DMSLKFDYPS VGQINNIASK
     NNFKIIFAVE KKVMRDYKAL EKKIQGSKYV ELKTGSKIVD MIKKEYLELV RTITLDAYNI
     PSLMELNYEP DCSSGACNVE HNKTLNIKGT LTVKSCPENK EVTHSLMIGP LSLNEKLNIE
     IEIDCECECE KVKNREENSK LCSENGTYQC GVCKCNENRS GDICQCVGNS VDTGDRNKCK
     ANNDIFPCSM FGTCRCGKCE CPKGFSGAYC EFNDNACPSP GGLICAGHGN CSFGRCICEP
     HWTGEGCKCP ENRCMAPYSQ EICSGNGDCV CGECKCKPMA NNNICSGKFC DDCEELAAKR
     CKELEEYAYC NYNANKTICD EKFNHTDTEV ILVNKTEIYS ADWYMAKMWC RKYLDDGRIL
     VFKYHYPNST TTSSLLLIIQ NELDMKSHVN LWIAGGSVLG SVLLIGLGTV LIWKVLIDMY
     DRREYQNFIK SSTAAGYNVE NVVYNPPIVT YRNPMCESK
//

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