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Database: UniProt
Entry: A0A3B1K3K6_ASTMX
LinkDB: A0A3B1K3K6_ASTMX
Original site: A0A3B1K3K6_ASTMX 
ID   A0A3B1K3K6_ASTMX        Unreviewed;      1112 AA.
AC   A0A3B1K3K6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Integrin subunit alpha 7 {ECO:0000313|Ensembl:ENSAMXP00000049083.1};
GN   Name=ITGA7 {ECO:0000313|Ensembl:ENSAMXP00000049083.1};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000049083.1, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000049083.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A3B1K3K6; -.
DR   Ensembl; ENSAMXT00000041475.1; ENSAMXP00000049083.1; ENSAMXG00000024694.2.
DR   GeneTree; ENSGT00940000159891; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000024694; Expressed in heart and 11 other cell types or tissues.
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; IPR018184; Integrin_alpha_C_CS.
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:SF90; INTEGRIN ALPHA-7; 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.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
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:UP000018467};
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:RU003762};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003762}.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           41..1112
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017207996"
FT   TRANSMEM        1049..1074
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   REPEAT          45..110
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          317..378
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          379..434
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          438..497
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          482..646
FT                   /note="Integrin alpha first immunoglubulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF08441"
FT   DOMAIN          648..805
FT                   /note="Integrin alpha second immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20805"
FT   DOMAIN          815..1041
FT                   /note="Integrin alpha third immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20806"
FT   REGION          896..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..939
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1112 AA;  122649 MW;  4937DA873377F421 CRC64;
     MCREDSAMDL QSTHRRTAGL TGPLVLLVLL LLALTAPTSA FNLDTTDTLN KEGEVGSFFG
     FSLALHQQLS PQPKSWLLVG APRARGLGAL RNSHPGALYR CPITAEEYDC ERVDIDGDVS
     LDRESKDNQW LGVTVKSQGI GGKVVACAHL YELRQRVNQL SETRDPIGRC YMLSEDLTER
     DDLDGGEWKF CEGRPQGHEQ FGFCQQGLAA SFTPDNNYVL FGAPGTYNWK GEMRVQQLNQ
     TLIHMGFYDD GPYEVAGEKQ QNAMLIPLPY HSYLGFSVDS AKGIMSRGEL TFVAGAPRAN
     HTGAVVLLKK DNVYRLVPEY ILWGEELASS FGYSVATTDL NSDGWTDLIV GAPNFFDRKA
     EIGGAVYVFL NPASHWEKAR PIRLNGTYDS MFGMTVSSVG DLDQDGYGDV AVGAPFDGDG
     KVFIFRGSAN GIDTKPSQVL DGLNAGVKRF GYSISGGLDI DGNLYPDLAV GSLSDQVVLY
     RSRPVIHVVR DISLEPQPID LTQQNCQGRD GVCVRIEACY TYTAHPETYS PHITLSVHFE
     ADTERRKLGL PHRVYFLGRA ASEPEYVHTK DLELRGQKHP ACQTATFVLQ ENIRDKLRPI
     SLAITHTIKK TRHQGHFGDK HLGRLSPVLG VSLSNTYYSE VNFLREGCGE DKICQSNLKL
     SYQFGTRAPT SDIFTPLPLD EDGVPVFSLS DQRSVVLEVT VSNTPSDPEN PQEDGDDAHA
     AQMVVTLPST LSYSGFRGQQ VVCQANQNGS QAECELGNPV KRDAVLKFYI ILSTSAITIE
     TTSLSVDLLM STISEQPGLT TVTAFAKVVI ELPLAVSGLA RPHQLFFSGE VRGESAMKTL
     DDVGSEVEYE FMVTNTGPSV QTLGSAFLNI MWPHELANGK WLLYPSGLHI EGHPQTHCTP
     KSALDPRGLR PKENHVQNLK ARRKTRSHPE EEEEEGKTMT KGGPPNTTPA VAASERRKSL
     KLDCLLGSAR CVLLQCPLHS FSGSALFRIS ARLWNTTFIE EFSAVSALEL LVRANITVKS
     SIKHLVLRDA AAQVPVMIYP EHGLSDQYWI PWWIILIAIL AGVLVLALLV CILWKCGFFK
     RTERHPHFET EYYRAHLQLQ PSDADKQAAE LQ
//
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