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Database: UniProt
Entry: A0A093CMN1_9AVES
LinkDB: A0A093CMN1_9AVES
Original site: A0A093CMN1_9AVES 
ID   A0A093CMN1_9AVES        Unreviewed;       740 AA.
AC   A0A093CMN1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
DE   Flags: Fragment;
GN   ORFNames=N339_03134 {ECO:0000313|EMBL:KFV14229.1};
OS   Pterocles gutturalis (yellow-throated sandgrouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX   NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV14229.1, ECO:0000313|Proteomes:UP000053149};
RN   [1] {ECO:0000313|EMBL:KFV14229.1, ECO:0000313|Proteomes:UP000053149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV14229.1};
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; KL244982; KFV14229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093CMN1; -.
DR   Proteomes; UP000053149; 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; 1.
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.
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:UP000053149};
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        692..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..50
FT                   /note="PSI"
FT                   /evidence="ECO:0000259|SMART:SM00423"
FT   DOMAIN          12..434
FT                   /note="Integrin beta subunit VWA"
FT                   /evidence="ECO:0000259|SMART:SM00187"
FT   DOMAIN          607..691
FT                   /note="Integrin beta subunit tail"
FT                   /evidence="ECO:0000259|SMART:SM01242"
FT   DOMAIN          715..740
FT                   /note="Integrin beta subunit cytoplasmic"
FT                   /evidence="ECO:0000259|SMART:SM01241"
FT   DISULFID        13..23
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        16..49
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        26..38
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        176..183
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        231..272
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        373..385
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        405..654
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        432..436
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        447..459
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        456..494
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        461..470
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        472..485
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        500..505
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        502..535
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        507..520
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        522..527
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        541..546
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        543..574
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        548..557
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        559..566
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        582..630
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        600..603
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        607..616
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        613..686
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   DISULFID        634..662
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV14229.1"
FT   NON_TER         740
FT                   /evidence="ECO:0000313|EMBL:KFV14229.1"
SQ   SEQUENCE   740 AA;  81648 MW;  E6420160ABC415EA CRC64;
     GSNICTTRGV NSCKQCLAVS PLCAWCSAEG LVPSSPRCDL HANLLQNGCR QDHIEFPTSS
     VTILEDRPLS NKGSGGSTTT QMSPQKIQLN LRPDDSQIFR VQVRQVEDYP VDIYYLMDLS
     NSMKDDLRNI QNLGTKLASE MRKLTSNLRI GFGAFVDKPI SPYMYISPPQ ALTNPCYEIR
     ETCLPMFGYK HVLSLTDEVT RFNEEVRKQN VSRNRDAPEG GFDAIIQATV CDEKIGWRND
     ASHLLVFTTD AKTHIALDGR LAGIVQPNDA QCHIDKDNFY SASTTLDYPS LGLMTEKLSQ
     KNINLIFAVT DTVVGLYQNY SELIPGTTVG TLSRDSSNVL QLIVDSYGKI RSKVELEVRD
     LPEELSLAFN ATCLNDEVIP GLKSCMGLKI GDTVSFSIEA KVRGCPRERQ KSFTIKPVGF
     KDSLTVVVNF NCNCSCESQA EANSSSCSQG NGTLECGVCR CNPGRLGSHC ECSEEEYNPS
     QQDNCSPQPG QPLCSQRGEC ICGQCMCHSS DFGKVTGKYC ECDDFSCVRF KGQMCSGHGQ
     CNCGDCLCDS DWTGDYCNCT TRTDTCMSSN GLVCSGHGSC VCGKGDRTQP GSYGDTCEKC
     PTCPDACTIK KECVECKKFE RGVLAEQQTC SRMCRDEIET VQELGDRGKD AVNCTYKDED
     DCVVRFQYYE DSSGKSILYV IEEPDCPKGP DVLVVLLSVT GAILLIGLTA LLIWKLLITI
     HDRREFARFE EEKARAKWDM
//
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