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Database: UniProt
Entry: A0A2Y9DH08_TRIMA
LinkDB: A0A2Y9DH08_TRIMA
Original site: A0A2Y9DH08_TRIMA 
ID   A0A2Y9DH08_TRIMA        Unreviewed;      1756 AA.
AC   A0A2Y9DH08;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN   Name=LOC101357545 {ECO:0000313|RefSeq:XP_004374205.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004374205.1};
RN   [1] {ECO:0000313|RefSeq:XP_004374205.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) 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       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   RefSeq; XP_004374205.1; XM_004374148.1.
DR   GeneID; 101357545; -.
DR   OrthoDB; 5475862at2759; -.
DR   Proteomes; UP000248480; Unplaced.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0048870; P:cell motility; IEA:InterPro.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   GO; GO:0031581; P:hemidesmosome assembly; IEA:InterPro.
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; IPR012013; Integrin_bsu-4.
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; PF07965; Integrin_B_tail; 1.
DR   Pfam; PF00362; Integrin_beta; 1.
DR   Pfam; PF17205; PSI_integrin; 1.
DR   PIRSF; PIRSF002513; Integrin_B4; 2.
DR   PRINTS; PR00014; FNTYPEIII.
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; 2.
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:UP000248480};
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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1756
FT                   /note="Integrin beta"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016160751"
FT   TRANSMEM        712..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1130..1219
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1223..1322
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1462..1557
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1575..1671
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          1667..1688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1756 AA;  195225 MW;  7BCCB0D2E8A6FB55 CRC64;
     MGGPRPSPWT RVLLVALLSI SFPGHMANHC KKAQVKSCTE CIRVGKDCAY CTDQMFKERR
     CNTQAELLAA GCRQESVVFM ESSFEITEET HIDTTLKRSQ VSPQGLRVWL RPGEERHFEF
     EVFEPLESPV DLYILMDFSN SMSDDLANLK QMGHNLAQVL RQLTSDYTIG FGKFVDKVSV
     PQTDMRPEKL KEPWPNSDPP FSFKNVISLT QDVEEFRSKL QGERISGNLD APEGGFDAIL
     QTAVCTRDIG WRPDSTHLLV FSTESAFHYE ADGANVLAGI MSRNDEECHL DASGTYTQYK
     MQDYPSVPTL VRLLGKHNII PIFAVTNYSY SYYEKLHTYF PVSSLGVLQE DSSNIVDLLQ
     EAFEAIRSNL DIRALDSPRG LRTEITSKMF PKTETGSFHI RRGEVGTYNV QLRAIEEVNG
     MHVCQLPAED HRGNIHLKPS FSDGLRMDVG IICDVCTCEL QKEVRSPLCS FNGDFTCGHC
     VCSEGWSGKT CNCSTGSLSD KQPCLREGED EPCSGRGECQ CGRCVCYGEG RYEGQFCEYD
     NLQCPRTSGF LCNDRGHCTM GQCVCEPGWT GPGCDCPLSN ATCTDSNGGI CNGRGHCECG
     RCHCNQQSLY TDTTCEINYS AIRLGLCEDM RSCVQCQAWG TGEKKGRPCE ECSFKVKMVD
     ELKKAEDVVE YCSFRDEDDD CTYSYTVEGD STPGPNTTVL VHNRKDCPPG SFWWLIPLLI
     FLLLLLALLL LLCWKYCACC KACLALLPCC NRGHMVGFKE DHYMLRENLM ASDHLDTPLL
     RSGNLKGRDT VRWKITNNVQ RPGFTTRSVS SNPTELVPYG LSLRLARLCT ENLLKPDTRE
     CEQLRQEVEE NLNEVYRQVT GDHKLQQTTF RQQPNAGKKQ DHTIVDTVLM APRSAKQALL
     SLTEKHVGQG AFHELKVAPG YYTLTADQDA RGMVEFQDGV ELVDVRVPLF IRPEDDDEKQ
     LLVEAIDVPS GTATLGRRLV NITIIKEQAS GVVSFEKPEY VVSHREQVAR IPIVRRIIDS
     GKSQVSYHTQ DNTAHGNRDY IPVEGELLFH TGETWKELQV KLLELQEMDS LLRGRQTRRF
     LIHLSNPKFG ARLGQPHSAT VIIGDGDEVD RSVTNWTLSS LPLVHSDPAA PQNPNAKAAG
     PRKIHFNWLP PPGKPTGYKV KYWIQGDSEA EAQVLDSKVP SVELTNLYPY CNYEMKVCAY
     GPQGESPYSS LVTCRTHQEV PSEPGRLAFN VVSSTVTQLS WAEPAETNGE ITAYEVCYGP
     VNEDNLPIGP MKKVLVDSPK RRMLLIENLR ESQPYRYTVK ARNGAGWGPE REAFINLATQ
     PKRPMSIPII PDIPIVDAQS GEDYNSFLMY SDDVLRSPSG SQRPSVSDDT EHLVNGRMDF
     TFPGSANSLH RMTVANAAYG THLSPHLPHR VLSTSSTLTR DYNSLTRTEH SHSQSATLPR
     DYSTLTSLSS HDSHMAAGVP NTPTRLVFSA LGPTSLKVSW QEPQCERALQ GYSVEYQLLN
     GDELHRLDIP NPSQTSVVVE DLLPNHSYVF RVRAQSQEGW GPEREGVITI ESQVHPQSPL
     CPLPGSAFTL STPSAPGPLV FTALSPDSLQ LSWERPRRPL GDILGYLVTC EIAHGGGPAT
     TFLVDGDSPE SRLTVPGLSE NVPYKFKVQA KTTQGFGPER EGIITIESQD GGPFPQPGSH
     PGLFQPSLPG EYSSVTTTTT HTNTTEPFLA DGLTLGSQHL EMGGSLTQHV TQEFVSRTLT
     TSGTLSTQVD HQFYHT
//
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