ID A0A8C1FH65_CYPCA Unreviewed; 795 AA.
AC A0A8C1FH65;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 3.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB1 {ECO:0000313|Ensembl:ENSCCRP00000091988.2};
OS Cyprinus carpio carpio.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000091988.2, ECO:0000313|Proteomes:UP001108240};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00000091988.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00000091988.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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 -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR AlphaFoldDB; A0A8C1FH65; -.
DR Ensembl; ENSCCRT00000099858.2; ENSCCRP00000091988.2; ENSCCRG00000045265.2.
DR GeneTree; ENSGT01150000286983; -.
DR Proteomes; UP001108240; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR GO; GO:0005925; C:focal adhesion; IEA:TreeGrafter.
DR GO; GO:0008305; C:integrin complex; IEA:TreeGrafter.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:TreeGrafter.
DR GO; GO:0019960; F:C-X3-C chemokine binding; IEA:TreeGrafter.
DR GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IEA:TreeGrafter.
DR GO; GO:0001968; F:fibronectin binding; IEA:TreeGrafter.
DR GO; GO:0005178; F:integrin binding; IEA:TreeGrafter.
DR GO; GO:0043236; F:laminin binding; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IEA:TreeGrafter.
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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; 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; 4.
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; EGF_integrin_1.
DR InterPro; IPR057073; EGF_integrin_2.
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; IPR057243; Integrin_I-EGF_CS.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082:SF62; INTEGRIN BETA; 1.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF23105; EGF_integrin; 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 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; 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 membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR002512-1};
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP001108240};
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 726..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..73
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 31..461
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 637..725
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 749..795
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 24..461
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 32..42
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 35..72
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 45..61
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 203..209
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 257..297
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 397..411
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 431..688
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 459..463
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 474..486
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 483..522
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 488..497
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 499..513
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 528..533
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 530..565
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 535..550
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 552..557
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 571..576
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 573..604
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 578..587
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 589..596
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 610..615
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 612..658
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 617..627
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 630..633
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 637..646
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 643..720
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 662..696
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 795 AA; 87705 MW; 9F86FABD40FA14AF CRC64;
MARSSNDGCF CCVRVCLCAD GNECTKASAQ SCGECIQAGE KCGWCIDKDF LKQGEQKSTR
CDEIEALIKK GCSEASIENP RGTVSVNKNQ SLTDRTKDGV KLKPDQITQI QPQKLTLNLR
SGEAQTFNLI FKRAEDYPID LYYLMDLSYS MKDDLENVKN LGTDLMAEMQ KITSDFRIGF
GSFVEKTVMP YISTTPAKLL NPCTSDQNCT SPFSYKNVLS LTSQGSQFNN LVSKQQISGN
LDSPEGGFDA IMQVAVCPNQ IGWRNVTRLL VFSTDAGFHF AGDGKLGGIV LPNDGKCHLQ
DNMYTMSHYY DYPSIAHLVQ KLSENNIQTI FAVTEEFQPV YQELKNLIPK SAVGTLSSDS
GNVIKLIIDA YNSLSSEIIL ENSRLPEGVS ISYISHCKNG VSDKGENGRK CSNISIGDQV
MFEVAIMAKG CPSNGKSETI KIKPQGFTEE VEIVLNFICE CACHKEGIPN SPVCHFGNGT
LECGACRCNE GRIGRVCECS KDEVRTDDLD ANCRMDNGTD ICNNNGDCVC GACECKKRDN
PEERYSGKFC ECDNFNCDRS NNKLCGGHGR CECRKCICEA NYTGSACDCS LDTSTCLASN
KQICNGRGTC ECGTCKCTDL KFQGPTCEIC PTCPGVCTEH KDCVQCQAFG TGEKKDTCKE
QCNKFILVKK KKKEELPQPN DQPYINHCKE RDANDCWFFF TYATKNDSTV EVHVAEELEC
PSGPDIIPIV AGVVAGIVLI GLALLLIWKL LMIIHDRREF AKFEKEKMNA RWDAGENPIY
KSAVTTVVNP KYEGK
//
