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Database: UniProt
Entry: A0A261C6N9_9PELO
LinkDB: A0A261C6N9_9PELO
Original site: A0A261C6N9_9PELO 
ID   A0A261C6N9_9PELO        Unreviewed;      1222 AA.
AC   A0A261C6N9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OZG18159.1};
DE   Flags: Fragment;
GN   ORFNames=FL83_07507 {ECO:0000313|EMBL:OZG18159.1};
OS   Caenorhabditis latens.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG18159.1, ECO:0000313|Proteomes:UP000216463};
RN   [1] {ECO:0000313|EMBL:OZG18159.1, ECO:0000313|Proteomes:UP000216463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX534 {ECO:0000313|EMBL:OZG18159.1,
RC   ECO:0000313|Proteomes:UP000216463};
RA   Fierst J.L.;
RT   "Caenorhabditis latens genome sequence.";
RL   Submitted (JUL-2017) 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: 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:OZG18159.1}.
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DR   EMBL; NIPN01000030; OZG18159.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261C6N9; -.
DR   STRING; 1503980.A0A261C6N9; -.
DR   Proteomes; UP000216463; Unassembled WGS sequence.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
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:SF133; INTEGRIN ALPHA-PS2; 1.
DR   Pfam; PF01839; FG-GAP; 3.
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   Pfam; PF00357; Integrin_alpha; 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; 5.
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:UP000216463};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU003762};
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..25
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   CHAIN           26..1222
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT                   /id="PRO_5011828176"
FT   TRANSMEM        1151..1173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   REPEAT          27..94
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          234..290
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          291..345
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          362..421
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          425..488
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          473..644
FT                   /note="Integrin alpha first immunoglubulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF08441"
FT   DOMAIN          646..794
FT                   /note="Integrin alpha second immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20805"
FT   DOMAIN          800..1139
FT                   /note="Integrin alpha third immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20806"
FT   REGION          896..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          978..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        929..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..1000
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1019..1034
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OZG18159.1"
SQ   SEQUENCE   1222 AA;  135538 MW;  DFE9B5EFF28BEE59 CRC64;
     MREGSFPRPT RLLCLLLGLF SLVAAFNIDT KNVVLHHMAN NYFGYSLDFY NEQKGMPVLV
     VGAPEAETTN PNLAGIRRPG AVYACSVNRP TCREVHVDKM KGNLKKLNGS HLVPIEDKAF
     QFFGATVKSN DKHDKLLMCA PKYKYFYSKF EVIEPVGTCF YAENGFDKTE EFSSCKQEPA
     RHGRHRLGYG QCGFSGAIPG KKNQDRVFLG APGVWYWQGA IFSQSTKNQT DRPNTEYGSK
     EYDHDMMGYS TATGDFDGDG IDDIVAGVPR GNDLHGKLVL YTSKLKMMIN LTDEVSTQHG
     QYCGGAVAVA DVNKDGKDDI IMGCPFYTDY GSVKDAKTQE RKPQYDVGKV IVFLQTAPGV
     FGKQIAVVGD DQWGRFGHSL AAAGDLNLDG YNDVIVGAPY AGKNKQGAVY VIHGSKDGVR
     EKPTQKIEAS QIGHGTARAF GFSVAGGVDV DGNGMPDIAV GAWKSGNAAV LLTKPVVTVT
     GATEPESALI NVEEKNCDVD AKLGKQACRH INTCFKYEGK GDTPNDLEFD LSFSLDDHSP
     EPRAYFLQKD VKGDRSIKVA SGSKTRDHPS SIEQRVRLEK GRQKCFRHRF FASSTMKDKL
     SPIHWSVNYT YVESKSGKLR GDKLEPAIDT TVPLSFQNKI NIANNCGKDD LCVPDLKVTA
     VADREKFLLG TQDNTMLINV TVQNGGEDSY ETKLYFDVPQ GFEYGGIETV GTDGSAPACS
     PTSDEPDSDG KWTFACDLGN PLPANKVVSS VVRVTASSDK PPLAPISINA HVNSSNDEEA
     HTIADNKVTF TIPVDFKNQL SLNGRSNPEQ VDFSMTNKTR PDVFDDNEIG PVVSHLYQIS
     NRGPSEIDAA TLDIFWPSFS TEGGHLLYII TEPVVNPPNK GRCRVKQLQN VNPLNLRITN
     EHVPTEPPVA KTPNEYSREE DDESYEDTTQ PQRTTSHRPS QHQTHQQGQV HVYERDEEKI
     RQNTGNWQYV EDKKKKGDYE YIPDEQEYDG PEFEDDEDED FDRAGSKRVK RSPVPKKKKK
     EGARSGEPRS EKARFSDLRE AVKLSKEAGG VVDYKGPLSR ASVDCNGLRC THIECDIYDL
     KEDEFVLVEI FSRLYTNTLV DERNPGGDIS SLALARVTST KYNLPHKPTL ITAVSTNMNA
     IASEEGRDLP WWLYLLAILI GLAILILLIL LLWRCGFFKR NRPPTEHAER RVDSQPAAHY
     ADTQARYASQ DQYNQGRHGQ ML
//
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