UniProt: A0A452H4B7

Database: UniProt
Entry: A0A452H4B7_9SAUR

LinkDB:  A0A452H4B7_9SAUR 
Original site:  A0A452H4B7_9SAUR

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Ontology (11)   
   GO (11)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (27)   
   InterPro (13)   
   Pfam (7)   
   PROSITE (3)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (42)   

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ID   A0A452H4B7_9SAUR        Unreviewed;      1676 AA.
AC   A0A452H4B7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JAN-2026, entry version 30.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000009324.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000009324.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2025) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSGAGP00000009324.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome
CC       {ECO:0000256|ARBA:ARBA00060371}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004193}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251,
CC       ECO:0000256|RuleBase:RU000633}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR   Ensembl; ENSGAGT00000010711.1; ENSGAGP00000009324.1; ENSGAGG00000006910.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR   GO; GO:0005925; C:focal adhesion; IEA:TreeGrafter.
DR   GO; GO:0030056; C:hemidesmosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008305; C:integrin complex; IEA:TreeGrafter.
DR   GO; GO:0005178; F:integrin binding; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:TreeGrafter.
DR   GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:TreeGrafter.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:TreeGrafter.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 3.
DR   FunFam; 2.10.25.10:FF:000212; Integrin beta; 1.
DR   FunFam; 2.10.25.10:FF:000215; Integrin beta; 1.
DR   FunFam; 2.10.25.10:FF:000287; Integrin beta; 1.
DR   FunFam; 2.60.40.10:FF:000424; Integrin beta; 1.
DR   FunFam; 2.60.40.2030:FF:000004; Integrin beta; 1.
DR   FunFam; 3.40.50.410:FF:000036; Integrin beta; 1.
DR   FunFam; 4.10.1240.30:FF:000003; Integrin beta; 1.
DR   Gene3D; 2.60.40.2030; -; 1.
DR   Gene3D; 4.10.1240.30; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
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; IPR038081; CalX-like_sf.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR040622; EGF_integrin_1.
DR   InterPro; IPR057073; EGF_integrin_2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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; IPR057243; Integrin_I-EGF_CS.
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; PF23105; EGF_integrin; 1.
DR   Pfam; PF23106; EGF_Teneurin; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF18372; I-EGF_1; 1.
DR   Pfam; PF07965; Integrin_B_tail; 1.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM00237; Calx_beta; 1.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00187; INB; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SUPFAM; SSF141072; CalX-like; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS00243; I_EGF_1; 1.
DR   PROSITE; PS52047; I_EGF_2; 2.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   ECO:0000256|RuleBase:RU000633};
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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        689..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1103..1192
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1196..1295
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1471..1600
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
SQ   SEQUENCE   1676 AA;  187078 MW;  2A0F234591F3E81D CRC64;
     VAELVGSTQV SCLLALALSK TIVLVLLFNR CVASRARSCT ECIRVSKDCS YCMDEVSASP
     PRTLSPTVCG EMLNFSLDLS LKKTQVSPQR MFMRLRAGEE ASFNMDVFQP LESPVDLYIL
     MDFSYSMSDD LNNLKEMGQK LAEFLQDLTS NYTIGFGKFV DKVSAPQTDM RPEKLREPWR
     DADSPFSFKN VIRLTSNINH FSQELMKERI SGNLDAPEGG FDAILQTAVC KEKIGWRTDS
     THLLVFSTES AFHYEADGTN VLSGILPRND EQCHLNRAGI YTYDTRQDYP SVPTLVRLMG
     QHNIIPIFAV TNHSYSYYEV KGFYLFIYVF FNTCLHLSLY NVRSLSPRGR QFKSTRAAAG
     SRRAVWPLAA NKRVSSIQGS FKVRVKAHEY MGGEHVCNLP KKEQQGVIHM KPSSLSDSLK
     IDVSVICDVC PCEQQKMVRS SMCSFNGDFV CGQCVCYPGW RGDMCDCSTA SSSDNQACIR
     PGDSEPCSGR GECLCGKCQC YSEDLTQRYE GNFCQFDNFQ CPRTSGFLCN DRGRCYMGQC
     ACESGWGGPG CECPTSNDTC IDSKGGICNG RGRCECGRCI CDKPSRYTDL TCEISYSLGV
     LGVCEDIRSC VQCQAWGTGE KKGQKCKDCS FKIQMVDELQ KAKEVNEYCS FQDEEDDCTY
     RYTLEGDPST VHNNTILVQK KKECPPGSFL WLIPLLIFLM LLLGLLLLLC WKYCTCCKPW
     SPLGFNLHPP LPAGRTVGFK EDHYMLRQSL MASDHLDTPM VRTGSLKGRD TVRWKINNNV
     HKPGFSSHTT TNPKELIPYG ISLRLARLFT QNLMKPDSRE CEQLRKEVEE NLNDVYKHVS
     GAHKLQQTKF RSAGKKGGQD HTIVDTVLTA PLSAKTEIVK VTEKHVSQEA FNELKVTPGY
     YTVTSDQDAH GMVEFQEGVE LVDVRVPLFI REEDDDEKQL QVEAIEVPTG TAAIGRRLVN
     ITIIKEQASS IITFLQPAYS HSRFDQVARI PVHREILENG KSQITYRTRD LTARDGKDYI
     FAEGDLVFQP GEMQKEVQVA LLELTEIDAL LQNRQLKQFA VDLLNPKYGA KIGKYPQTTV
     TITDPEAVDG IQFPQSPRGK LGAPLSPNAQ ALNSRKIRFN WLPPPGKPIG YKVKYWIQGD
     PESEARLINS TVPSAELNNL YPYCDYEMQV CAYSNMGEGP YSDITHCRTL EDVPSEPGRL
     AFNVVSSTVT QLSWAEPAET NGEIIAYEVS YGLVNEDNVP FGPMKKVLVE EPKKRMVLIE
     NLRESQPYRY TVKAKNGAGW GPEREATINL ATQPRRPMSI PIIPDIPIID AEGGEDYDSY
     LMYSADVMRS PCGSKRPSVS DDSEHLPNGR MDFTFPGSGG TLNRTLNASY NQLTSHVHQE
     RRLMGSSSLT RDYSTMTSGY GESQPGRILP SIHEDPGRMA LLPQDVGVRS RAKVKGSYAS
     NSFRDSIIMT DGSTGIAKYI DSRMALGVPD TPTRLVFSAL GPTSLKVSWQ EPQCEKEVQG
     YSVQYQLLSG GQRETSLHGT GGCLFPALPQ TSWVAPHALV FLFGLGEPRN IYVEGDNPET
     SLTVPYLSEN IPYKFKVQAK TTQGFGPERE GIITIESQDG GTTFLDVYNL PAEYNTTTTI
     SHSSLEPYYT DGMLMTTQRV ESSGTLTKQV TKEFVSRTMM SSGTLTKQME AQFFEA
//

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