ID A0A077ZDE1_TRITR Unreviewed; 1008 AA.
AC A0A077ZDE1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Protein ina fg gap protein {ECO:0000313|EMBL:CDW56610.1};
GN ORFNames=TTRE_0000489001 {ECO:0000313|EMBL:CDW56610.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW56610.1};
RN [1] {ECO:0000313|EMBL:CDW56610.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW56610.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU003762}.
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DR EMBL; HG806059; CDW56610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZDE1; -.
DR STRING; 36087.A0A077ZDE1; -.
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:SF122; INTEGRIN ALPHA-PS1; 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; 4.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 2.
DR PROSITE; PS51470; FG_GAP; 3.
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 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 860..882
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT TRANSMEM 957..981
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 187..249
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 277..338
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 348..410
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 395..540
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 542..690
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 696..826
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
FT REGION 819..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1008 AA; 112966 MW; C30EE969FFCC46F9 CRC64;
MNTLISAYMH LVWAVCAPNL IYDMAYIEGA CFLLRNDLSH VKRIRTCQGF TKKNRHNDYG
VCQEGFSAAL SEKHEVIATG LPGASRWTGG AFAQDIDEAQ STLHSRWTAT VRGDHAVESV
VKAHSYFGYS INVGIFGFWY EKAGRNGNLT LVAGCPRCNE TGAVYFMPFS KEVTVNDYSA
LRLLSDHFNL TGDEWFASGF GYSVGVVDIN GDGFDDLLVG APYFYGITST EVYGGRAYVY
FSIGSKQVLS ETWLCFIPRF CIAYAFQSKD LNAHVFQEAI RLSGPKDSMF GASVANLGDI
NNDKFNGALL QNIAIGAPYH DDGGAVYIYL GAEASDFERK PIQVILGNKL HLSPLSKPLE
TFGWSLSGGT DLDNNGYPDL LVGAFKSDVA VLLRARPIVH VVALVEETDL TPIDVDEQYC
SEHWAKACVR FHTKLRVKRQ AVLSHGSSAL RAEFAHGAKY EREWACGKGA VEQPQEKEHE
LFIRDSNRDW LNPLKFEFSV SLSKSKPSFS REAVSLPDIN DHPVLDKKGS KKEFMIEFNK
KCGPDNKCVS DLALQCFFVD LARESKSDVY VKQVGKDDEL DLQYRLLNKG ERAYESSLFV
LYNEDELERP MLLQKAHYGL NFGKFENGLI EVLLGNPLEA MAEIVFSLRF KLTRGRSEGL
GDVLVFDSYV NSTSMEKYED DNRCKASVKV IKKAELEIVG TSDPQLVYFG GKSFGQSAVE
YEEDIGPQVV HTYLVRNGGP WGVNDVTVTI DHPYQISDMH VRGKWALYLM YLPIIELPIP
GSTTTETRNC YVDSMAEYVN PLEIKIGSAE DEIEGMRIEG GKGKQSSEKV GKDSISSGSS
MREFRAPTET IEEGGETLVY IIRTSFALVR IVYIILNTFA LLLKSGSSYY LYILFSASVP
VFRQDYRHVD HLLIESHGTV DMKRFQGIEE TNYLDNEATA VTRVQPDMPK IAEKKRVPLW
IIILAILGGI FLLLLVTILL WKCGFFKRGK YYDKPLYTAE YKRSDDYD
//