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Database: UniProt
Entry: A0A091NJ51_9PASS
LinkDB: A0A091NJ51_9PASS
Original site: A0A091NJ51_9PASS 
ID   A0A091NJ51_9PASS        Unreviewed;      1817 AA.
AC   A0A091NJ51;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN   ORFNames=N310_01673 {ECO:0000313|EMBL:KFP79242.1};
OS   Acanthisitta chloris (rifleman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC   Acanthisitta.
OX   NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP79242.1, ECO:0000313|Proteomes:UP000053537};
RN   [1] {ECO:0000313|EMBL:KFP79242.1, ECO:0000313|Proteomes:UP000053537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP79242.1};
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; KK834797; KFP79242.1; -; Genomic_DNA.
DR   Proteomes; UP000053537; 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   CDD; cd00063; FN3; 4.
DR   Gene3D; 2.60.40.2030; -; 1.
DR   Gene3D; 4.10.1240.30; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; IPR038081; CalX-like_sf.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR040622; I-EGF_1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR033760; Integrin_beta_N.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR012896; Integrin_bsu_tail.
DR   InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR   InterPro; IPR002369; Integrin_bsu_VWA.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR   PANTHER; PTHR10082:SF42; INTEGRIN BETA-4; 1.
DR   Pfam; PF03160; Calx-beta; 1.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF18372; I-EGF_1; 1.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00237; Calx_beta; 1.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SUPFAM; SSF141072; CalX-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR   SUPFAM; SSF103575; Plexin repeat; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS00243; INTEGRIN_BETA; 2.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|RuleBase:RU000633};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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:UP000053537};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1817
FT                   /note="Integrin beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001878899"
FT   TRANSMEM        715..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1133..1222
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1226..1325
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1526..1619
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1639..1735
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          1402..1440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1817 AA;  203645 MW;  4B6EFECACD28BC1B CRC64;
     MDVLPRVCAG LLLLSLLCAT GLCQWSKNNR CVLSRAKNCT ECIRVDKDCS FCADESFEEP
     RCDLRENLLR YGCAETSIMY SRGGMWTQKN TSINTFLQRT QVSPQGMAMN LRAGEEMSFN
     MDVFQPLESP VDLYILMDFS YSMSDDLNNL KSMGHNLAAF LQDLTSNYTI GFGKFVDKVS
     SPQTDMRPQK LLEPWHKADS PFSFKNVIRL TSNIDYFNEK LQKERISGNL DAPEGGFDAI
     LQTAVCKDKI GWRKDSTHLL VFSTESAFHY EADGTNVLAG ILARNDEQCH LDTHGTYVYD
     TKQDYPSVPT LVRLLGRHNI IPIFAVTNHS YSYYQKLHKY FPISEIGVLQ EDSSNIVELI
     RTAFERIRSK MDIRADFTPK AIKTEFTSSM YEKTESGSFH ITRGEVGKFN MHVKALEYVG
     GQHVCSLPEK DRKGVIHVKP TSLSDSLTVE TSVVCDVCTC EQQKEWSSPK CSFHGDFVCG
     QCICHQGWRG DTCDCSPEVS SNNEGCIRPG DVEPCSGRGE CLCGKCQCYS EDLTQRFDGE
     FCQYDVLQCP RSSGFLCNDR GRCSKGACVC ESGWEGPGCE CPTSNDTCID SRGGICNNHG
     RCECGRCICD MASLYTSSTC EISYSLGFQA VCDSIRDCVT CQTWGTGNKK GNCSTCHLQI
     QMVEELKKEE AGEYCSFQDE DDDCTYHYTL EGDPSVLPNT TVRVQKNKEC PPATFFWLIP
     LLIFLILLLG LLLLLCWKFC ACCKTCLALL PCCARGRTVG FKEDHYMLRH SLMSSDHLDT
     PMVRSGSLKG RDTVRWKIHN NVHKQSFTSP TATSPKDLVP YGLSLRLARL FTQNLMKPDT
     RECEQLRKEV EENLNDIFKH IPGCHKLQQT KFRLQPNSGK RQDHTIVDTV LTAPRSAKSD
     IIKAVEKHVS HEAFNDLKVA PGYYTVTSDQ DAQGMVEFQE AVELVDVRVP LFIREEDDDE
     KQLQVEAIEV PNGIAKIGRR VVNITIIKEQ ASSLITFLQP AYSHSRFDKL AKIPVLREII
     DNGKSQVTYR TRDLTAKDGR DYIFTEGGLP FQPGETRKEI QVPLLELTEI DTLLNNYQLK
     QFAIDLIHPK YGAKIGRYPQ TTVTIADPEL VDGVSSMSGM GQIHQSTKTY LSAPYNPKAT
     ALSSREINFN WCPPPGKPLG YKVKYWIQGD SESEANLMDV KTPPAALTNL YPFCDYEMRV
     CAYNAAGEGD YSDIIHCRTL EEVPSEPGRL AFNVVSSTVT QLSWAEPAET NGEITAYEVS
     YGLVNEDNEP FGPMKKVLVE DPKKRMVLIE NLHESQPYRY TVRARNSAGW GPQRAATINL
     ATQPKRPMSI PIIPDIPIID AEGGEDYDSY LMYSTDVLRS PAGSKHPSVS DDTGSRWKYV
     PLLGEDLDLR RITWRLPPET IPRLSGSSRL SSDTEGLLHE EDSDVAPGSL RRSGTPRPQA
     EHLLNGRVDF CYPGSGSGTL TRMMNTSYHQ LNSHMHQEHR VMGSSSLTRD YSTMQMGHGD
     LCLHHTTFPF AGDFHYSRKP LGIPDTPTRL VFSALGPTSL KVSWQEPRCE KEVKGYSVQY
     QLLNGGEVHR ISIPDPRQNS VVVEDLLPNH SYIFRVKAQS EEGWGPDREG VITIESQVDP
     QSPLSPVPGT PFTLSTPCAP GPLVFTALSP DSLHLSWERP REPNGPILGY RITCEMLHGG
     GEPRTIYVEG DNLETTLTVP HLSENVPYKF KVQANTTQGF GPEREGLITI ESQDRGAFSQ
     LGGQQYVREE VYKFPTEYST KTSISHSSLD PHFTDGMLMT TQRVENTSST LTQEFVSRTV
     MSSGTLTKQV ERQFYEA
//
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