ID A0A3L8QB65_CHLGU Unreviewed; 1143 AA.
AC A0A3L8QB65;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RLV64459.1};
GN ORFNames=DV515_00017470 {ECO:0000313|EMBL:RLV64459.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV64459.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLV64459.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLV64459.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLV64459.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV64459.1}.
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DR EMBL; QUSF01001175; RLV64459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8QB65; -.
DR STRING; 44316.ENSEGOP00005011568; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR InterPro; IPR048286; Integrin_alpha_Ig-like_3.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF89; INTEGRIN ALPHA-3; 1.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF08441; Integrin_A_Ig_1; 1.
DR Pfam; PF20805; Integrin_A_Ig_2; 1.
DR Pfam; PF20806; Integrin_A_Ig_3; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 3.
DR PROSITE; PS51470; FG_GAP; 4.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003762};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003762};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003762}.
FT TRANSMEM 1066..1090
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 34..97
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 287..348
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 349..404
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 408..470
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 455..604
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 605..750
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 759..929
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 861..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1143 AA; 125794 MW; BA72239E61B94751 CRC64;
MARRRRLLPP PLPGLLLGLG PVLLGAAAAF NLDRTFPVLK EGPAGALFGF SVALHRETER
RDRSLLLVGA PQDAEPVNGT RTGAVYACPL SAATRDCQRL AIELKDEPDK AIIEDMWLGV
TVASQRQPPG RVLACAHRYT RVLWSGAEAQ RRMVGRCYVR GNDLLLDLGD EWQTYHNEMC
NANTDTDETG MCQMGTSAGF GANIIYFGAP GAYNWQGTDY MLQRDSWDLH DFSYPNKRNG
NTYIGYTAEV GSALLQRDAV TVVTGAPRYR HTGAVLLLSR GARQALNRSL LLPGPQVGSY
FGSALALADL NNDGWQDLVV GAPYYFERKQ EVGGAVFVYM NEAGGFQQLP SLVLTGPSYS
GFGFALASVG DINQDGFQDI AVGAPFEGPG KVYIYHSSAE GLRDRPRQVI SGSDLGPTTI
KTFGYSLSGG LDTDGNSYPD LLVGSLSERV VLLRARPVIN ILDKTFTVTP SKVDPAQCTP
NMTVTLCFSY NQSAGDPSYS ERITLQYTLE ADKDRHPPRV RFAGSQSATY TGDFSMPDTR
CQSQELLLLD NVRDKLHPIV LSMNYSLLER PRTFQLGPHS LDAFPVLNQD QSHENETKIE
FQKECGSDNQ CYSNLQLQSS FVTEQNQPLP RVNGTQVLQY SRDVRKLHLG INISNVPTAP
WNGEDAHEAL LNVTVPPSLL PSSVRPSGAC TFGDTVLCEL GNPFKRNQRA ELTITFEAIG
IMLDTREVDV WLDLSTQSTQ EDLQPVLAKL LVDYSIQSSL SIASSHIQSY FSGTVVGESA
MKQEQDVGSP LTFDFQVTTK GESLGTLGTI LLGFEWPYEI PNGKWLLYPT EILVNGNDTC
HPPGGVINPL NLTLLQDRAA ARRRRELEPP EPGEPPVTLA TGRRPRSEAA LSCSAGTARC
VWFECPLLHT QLPSSFSLRA RVWNSTFIEV SAGAAGPGLP EPRGGVKRGP EPARAQLRSW
HPPRGVPAVT CVPPPSVCHP SSMSPSSSTS PSSSSTCCRL CVPAHPRPSA VSPCPQEFRD
FDRVKVTGTA TLFLRSQVPT ITMRNHTVRF SVDVDSELQE EQPAEIALWL VLVSVAAGLL
LLGLIILLLW KCDFFQRTRY YRIMPKYHAV RIRQEQRYQP GGLLPRRRKK LWVTKWQEPD
KYY
//
