ID A0A3Q1H145_ANATE Unreviewed; 1128 AA.
AC A0A3Q1H145;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Integrin alpha-M-like {ECO:0000313|Ensembl:ENSATEP00000000900.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000000900.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000000900.2}
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; A0A3Q1H145; -.
DR Ensembl; ENSATET00000000918.2; ENSATEP00000000900.2; ENSATEG00000000538.2.
DR GeneTree; ENSGT00940000154838; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 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; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR048633; ITGAX-like_Ig_3.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF134; INTEGRIN ALPHA-L ISOFORM X1; 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; PF21520; ITGAX-like_Ig_3; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00191; Int_alpha; 4.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 2.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS51470; FG_GAP; 3.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003762};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
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 1038..1059
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT DOMAIN 148..323
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 430..492
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 493..549
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 554..614
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REGION 1074..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1128 AA; 125282 MW; FD8452D896529B24 CRC64;
MVVLAIPVSL SFNIEITNPS VYTGKKEDFF GYKVLQFTSG SNKGIIVTAP LQLNGTGGVC
NPGQNLSHPC FNSQEISVEN QMIPVKHLGL SIAADPKGSN FTVCSPSVAH ECDENSYLNS
VCYTVTYDLQ QASSSTPAFK ECRKKTVDLV FLFDGSGSMT EAEFNKNKDF IVDIINSLKN
SSIKFAAVQF STYYSKVFDF NDYQAGTALD KLHKEPHMKT LTNTHRALRF VLEDILENPA
AGASADATKV LVLITDGDPS DTDRYGIIQR YDEMNIIRFV IMVKAAKQDK FTHIASQPTV
KYAFKIENYD GLTGILENFQ KQIFEMEGSK AALAGNMTNE MSQSGFSAVV YNGALILGSV
GSNGWRGSLQ EFHNQKETQI EDPDMQVDSY MGYSISVAKK NNDLLYFTGA PRFEHSGQVT
VFRQNDTKWT PAQSLKGDMI GSYFGAELCS VDIDSDGNTD FLLVGAPLFY HPQEKREGQI
YVYTLTDEMQ LTIEQNVTVS SMGRFGTSIS SIADLNGDGL RDVAVGAPLE DDNSGAVYIY
LGDRRTGIRS TFSQRIMGQR IKPGLRLFGQ AIDGTIDMGE DGLPDIVIGS QGTAVVLRSK
PVFNVTSRLS FLPGEIVIEK FDCTGGNKEV LPMVTLTVCF EMTEHEPLNR CCSGLNISYT
LDVDPMRQTY RGLFSSSDNK ARSITSSCVL RDDETCLNHT IYMPTCVKDL LSPVSVKLNL
TQTDSDAENV LNVDSEKQCR KNDTCIADLV VDFNFLTPTL LVAENNKFDI SVKLSNPGDD
SYNTSLIMHY PAGLSFSMMV LTESTRPTLH RCDDLKGVLD KTVCGVSRPV YRRGSSVSHT
APTQQTEVMK KDTISYLNFT TEDSAPKKVE ITYKIDNPGS RSFPVHVSVV FPAELDYNFE
MKNYQVLVEK NKTQCTNVKS NLCPSEKSSK IIKCDPFILD KATELKLIGD VHFKDLKQHA
ANLAFLKRYV GDGGKVKFKS FIHVSYDEKR YVLDSGKKEN KDPTKKRSNE TCLWEESGPT
VKWTEIQVEF IIPVDQQLIV LTGVVLGLLF LIILTVIMWK MGCFKRRKLP DTEERESLQS
NNYAPSQPTP VPTTETNSKS NNDSKSEEPS EENKPLKNNE LEKDQGGH
//
