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Database: UniProt
Entry: F1KYS4_ASCSU
LinkDB: F1KYS4_ASCSU
Original site: F1KYS4_ASCSU 
ID   F1KYS4_ASCSU            Unreviewed;       720 AA.
AC   F1KYS4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   22-FEB-2023, entry version 42.
DE   SubName: Full=Protein unc-112 {ECO:0000313|EMBL:ADY43028.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY43028.1};
RN   [1] {ECO:0000313|EMBL:ADY43028.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
CC   -!- SIMILARITY: Belongs to the kindlin family.
CC       {ECO:0000256|ARBA:ARBA00008052}.
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DR   EMBL; JI168192; ADY43028.1; -; mRNA.
DR   AlphaFoldDB; F1KYS4; -.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 2.
DR   CDD; cd13205; FERM_C_fermitin; 1.
DR   CDD; cd17095; FERM_F0_kindlins; 1.
DR   CDD; cd01237; PH_fermitin; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR037843; Kindlin/fermitin.
DR   InterPro; IPR040790; Kindlin_2_N.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR037837; PH_Kindlin/fermitin.
DR   PANTHER; PTHR16160; FERMITIN 2-RELATED; 1.
DR   PANTHER; PTHR16160:SF13; FERMITIN 2-RELATED; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF18124; Kindlin_2_N; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889}.
FT   DOMAIN          403..508
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          150..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   720 AA;  81735 MW;  029ADFCE1EB6BE40 CRC64;
     MAHLVENGVV NDGSWSLSVL VTDMNIQRTL FVTGQLHIGG LMLKLVDEID VTRDWSDHAL
     WWPEKRKWLT HTRSTLDQMG ITADCSLEFT PQHKLARVQL PDLQMIDARL DFSVNVVKAT
     QQLCREIGIR YSEELSLKRF IPPEMLRKGL GFESDQSGPQ PIRPGEESIG PGTLRRQTPI
     SASACNLAGP LRRGTSPSLS TSGQMFNASE LGTLPRSGTL PRGVSPGPAA YSGTIGRTPM
     MPSVSFCEGL ENEQYDMALV HSPRIVPNKE MTVFRPQNYI EKAALNRGWL DSSRSLMEQG
     VFEGDVILLR FKFMTFFDMN PKYDPVRINQ LYEQAKWSIL LEEYDHTEEE AMLFAALQLQ
     ATLQRNSPEP DPTERDDVDV LLDELEQNLD AAALSRRSDL TQVPELADYL KYMKPKKLAA
     FKGFKRAYFS FRDLYLSWHQ NSNDISGPPL GHICLKGCEV NPDVSLAQSK FHIKLLIPSA
     EGMSEFVLKC DTEHQYARWM AACRLASRGK SMADASYQSE VDSIKKLLQM QSGVTGSAQN
     GTSKKKAPPV QLPPDFNVDE FVSQRYVRRA RSKQSLQQRI SDAHSNVRSL SSTEAKLQYI
     RAWEALPEHG THYFVVRFRN GRKPELIGIA FNRIMKLNID SGESLKTWRF ATMKKWHVNW
     EIRHLKIQFE NEDIEFKPLS ADCKVVHEFI GGYIFLSLRN KEQSQTLNEE LFHKLTGGWA
//
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