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Database: UniProt
Entry: A0A093NDC2_PYGAD
LinkDB: A0A093NDC2_PYGAD
Original site: A0A093NDC2_PYGAD 
ID   A0A093NDC2_PYGAD        Unreviewed;       768 AA.
AC   A0A093NDC2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
DE   Flags: Fragment;
GN   ORFNames=AS28_00888 {ECO:0000313|EMBL:KFW62928.1};
OS   Pygoscelis adeliae (Adelie penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX   NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW62928.1, ECO:0000313|Proteomes:UP000054081};
RN   [1] {ECO:0000313|EMBL:KFW62928.1, ECO:0000313|Proteomes:UP000054081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW62928.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC       ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004251, 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; KL224723; KFW62928.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093NDC2; -.
DR   STRING; 9238.A0A093NDC2; -.
DR   Proteomes; UP000054081; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.1240.30; -; 1.
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; 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; IPR012896; Integrin_bsu_tail.
DR   InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR   PANTHER; PTHR10082:SF25; INTEGRIN BETA-3; 1.
DR   Pfam; PF07974; EGF_2; 2.
DR   Pfam; PF18372; I-EGF_1; 1.
DR   Pfam; PF08725; Integrin_b_cyt; 1.
DR   Pfam; PF07965; Integrin_B_tail; 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; SM00187; INB; 1.
DR   SMART; SM01241; Integrin_b_cyt; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SMART; SM00423; PSI; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000054081};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000633};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        698..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          10..56
FT                   /note="PSI"
FT                   /evidence="ECO:0000259|SMART:SM00423"
FT   DOMAIN          18..440
FT                   /note="Integrin beta subunit VWA"
FT                   /evidence="ECO:0000259|SMART:SM00187"
FT   DOMAIN          613..697
FT                   /note="Integrin beta subunit tail"
FT                   /evidence="ECO:0000259|SMART:SM01242"
FT   DOMAIN          721..767
FT                   /note="Integrin beta subunit cytoplasmic"
FT                   /evidence="ECO:0000259|SMART:SM01241"
FT   REGION          72..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        19..29
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        22..55
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        32..44
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        182..189
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        237..278
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        379..391
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        411..660
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        438..442
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        453..465
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        462..500
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        467..476
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        478..491
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        506..511
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        508..541
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        513..526
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        528..533
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        547..552
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        549..580
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        554..563
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        565..572
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        586..591
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        588..636
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        593..603
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        606..609
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        613..622
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        619..692
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        640..668
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW62928.1"
FT   NON_TER         768
FT                   /evidence="ECO:0000313|EMBL:KFW62928.1"
SQ   SEQUENCE   768 AA;  84766 MW;  DCB59B2AC57F3C96 CRC64;
     LCFAVSGGNI CTTRGVNSCK QCLAVSPLCA WCSAEDLPQS SPRCDLRTSL LQNGCGQEYI
     EFPTSTVTIL EDRPLSNKGS GSSTTTQMSP QKIQLNLRPD DSQIFRVQVR QVEDYPVDIY
     YLMDLSNSMK DDLRNIQNLG TKLASEMRKL TSNLRIGFGA FVDKPISPYM YISPPQAITN
     PCYEIGETCL PMFGYKHVLS LTDEVTRFNE EVRKQSVSRN RDAPEGGFDA IIQATVCDEK
     IGWRNDASHL LVFTTDAKTH IALDGRLAGI VQPNDAQCHI DKDNFYSAST TLDYPSLGLM
     TEKLSQKNIN LIFAVTDTVV GLYQNYSELI PGTTVGTLSR DSSNVLQLIV DSYGKIRSKV
     ELEVRDLPEE LSLAFNATCL NDEVIPGLKS CMGLKIGDTV SFSIEAKVRG CPRERQKSFT
     IKPVGFKDSL TVVVNFNCDC SCESQAEANS SSCSRGNGTL ECGVCRCNPG RLGSHCECSE
     EEYNPSQQDN CSPQPGQPLC SQRGECICRQ CVCHSSDFGK VTGKYCECDD FSCVRFKGQM
     CSGHGQCNCG DCLCDSDWTG DYCNCTTRTD TCMSSNGLVC SGHGSCVCGK CDCTQPGSYG
     DTCEKCPTCP DACTIKKDCV ECKKFERGVL MEQQSCSRMC RDEIETVQEL GDRGKDAVNC
     TYKDEDDCVV RFQYYEDSSG KSILYVIEEP DCPKGPDVLV VLLSVTGAIL LIGLAALLIW
     KLLITIHDRR EFARFEEEKA RAKWDTGHNP LYKEATSTFT NITYRGNM
//
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