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Database: UniProt
Entry: E2ITE0_HUMAN
LinkDB: E2ITE0_HUMAN
Original site: E2ITE0_HUMAN 
ID   E2ITE0_HUMAN            Unreviewed;       493 AA.
AC   E2ITE0;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   28-JUN-2023, entry version 34.
DE   SubName: Full=CABYRa {ECO:0000313|EMBL:ADK33598.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:ADK33598.1};
RN   [1] {ECO:0000313|EMBL:ADK33598.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Nasopharynx {ECO:0000313|EMBL:ADK33598.1};
RA   Yang C.-Y., Tseng Y.-T.;
RT   "Aberrant expression of the sperm fibrous sheath protein CABYR in human
RT   cancers and identification of alpha-enolase as one of CABYR-interacting
RT   proteins.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HM594166; ADK33598.1; -; mRNA.
DR   AlphaFoldDB; E2ITE0; -.
DR   PeptideAtlas; E2ITE0; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048240; P:sperm capacitation; IEA:InterPro.
DR   CDD; cd12100; DD_CABYR_SP17; 1.
DR   Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR   InterPro; IPR038848; CABYR.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR047579; DD_CABYR_SP17.
DR   PANTHER; PTHR15494; CALCIUM-BINDING TYROSINE PHOSPHORYLATION-REGULATED PROTEIN; 1.
DR   PANTHER; PTHR15494:SF0; CALCIUM-BINDING TYROSINE PHOSPHORYLATION-REGULATED PROTEIN; 1.
DR   Pfam; PF02197; RIIa; 1.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
PE   2: Evidence at transcript level;
FT   DOMAIN          12..49
FT                   /note="RIIa"
FT                   /evidence="ECO:0000259|SMART:SM00394"
FT   REGION          85..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..163
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        426..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  52714 MW;  ADAF39DB64E143B7 CRC64;
     MISSKPRLVV PYGLKTLLEG ISRAVLKTNP SNINQFAAAY SQELTMYRGN TTMDIKDLVK
     QFHQIKVEKW SEGTTPQKKL ECLKEPGKTS VESKVPTQME KSTDTDEDNV TRTEYSDKTT
     QFPSVYAVPG TEQTEAVGGL SSKPATPKTT TPPSSPPPTA VSPEFAYVPA DPAQLAAQML
     GKVSSIHSDQ SDVLMVDVAT SMPVVIKEVP SSEAAEDVMV AAPLVCSGKV LEVQVVNQTS
     VHVDLGSQPK ENEAEPSTAS SVPLQDEQEP PAYDQAPEVT LQADIEVMST VHISSVYNDV
     PVTEGVVYIE QLPEQIVIPF TDQVACLKEN EQSKENEQSP RVSPKSVVEK TTSGMSKKSV
     ESVKLAQLEE NAKYSSVYME AEATALLSDT SLKGQPEVPA QLLDAEGAIK IGSEKSLHLE
     VEITSIVSDN TGQEESGENS VPQEMEGKPV LSGEAAEAVH SGTSVKSSSG PFPPAPEGLT
     APEIEPEGES TAE
//
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