ITPI2_PONAB
ID ITPI2_PONAB Reviewed; 768 AA.
AC Q5REU9; Q5REV0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Protein ITPRID2 {ECO:0000305};
DE AltName: Full=ITPR-interacting domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Sperm-specific antigen 2 homolog {ECO:0000250|UniProtKB:P28290};
GN Name=ITPRID2 {ECO:0000250|UniProtKB:P28290};
GN Synonyms=SSFA2 {ECO:0000250|UniProtKB:P28290};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Located near the
CC plasma membrane. Associated with actin filaments. May also exist as a
CC membrane-bound form with extracellular regions (By similarity).
CC {ECO:0000250}.
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DR EMBL; CR857416; CAH89707.1; -; mRNA.
DR EMBL; CR857417; CAH89708.1; -; mRNA.
DR RefSeq; NP_001124775.1; NM_001131303.1.
DR RefSeq; NP_001128928.1; NM_001135456.1.
DR AlphaFoldDB; Q5REU9; -.
DR SMR; Q5REU9; -.
DR STRING; 9601.ENSPPYP00000014512; -.
DR GeneID; 100189884; -.
DR KEGG; pon:100189884; -.
DR CTD; 6744; -.
DR eggNOG; ENOG502QSG8; Eukaryota.
DR InParanoid; Q5REU9; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR InterPro; IPR026648; ITPRID2.
DR InterPro; IPR029326; SSFA2_C.
DR InterPro; IPR043444; TESPA1-like.
DR PANTHER; PTHR17469; PTHR17469; 1.
DR PANTHER; PTHR17469:SF11; PTHR17469:SF11; 1.
DR Pfam; PF14723; SSFA2_C; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..768
FT /note="Protein ITPRID2"
FT /id="PRO_0000280707"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 468..546
FT /evidence="ECO:0000255"
FT COMPBIAS 39..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922B9"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922B9"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922B9"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q922B9"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 665
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT MOD_RES 677
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P28290"
FT CONFLICT 25
FT /note="T -> I (in Ref. 1; CAH89707)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="R -> G (in Ref. 1; CAH89707)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="N -> S (in Ref. 1; CAH89707)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="E -> G (in Ref. 1; CAH89707)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="I -> V (in Ref. 1; CAH89707)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="L -> Q (in Ref. 1; CAH89708)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="G -> R (in Ref. 1; CAH89708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 768 AA; 84713 MW; 2D86D17B411D8A62 CRC64;
MTTEDHLLRT ASQHSDSSGF AEDSTDCLSL NHLQVQESLQ AMGSSADSCD SETTVTSLGE
DLATPTAQDQ PYFNESEEES LVPLQKGLEK AAAIADRRKS GSQDFPQCNT IENPGTKQST
CSPGDRVTEI TEVEEDLFPA ETVELLREAS AESDVDKSSE CEFTQYTTHH ILKSLASIEA
KCSDMSSENT TGPPSSVDRV NTALQRAQMK VCTLSNQRMG RSLLKSKDLL KQRYLFAKVG
YPLRRSQSLP TTLLSPVRVV SSVNVRLSPG KETRCSPPSF TYKYTPEEEQ ELEKRAMEHD
GQSLVKSTIF ISPSSVKKEE APQSEAPRVE ECHHGRTPTC SRLAPPPMSQ STCSLHSIHS
EWQERPLCEH TRTLSTHSVP NISGATCSAF ASPFGCPYSH RHATYPYRVC SVNPPSAIEM
QLRRVLHDIR NSLQNLSQYP MMRGPDPAAA PYSTQKSSVL PLYENTFQEL QVMRRSLNLF
RTQMMDLELA MLRQQTMVYH HMTEEERFEV DQLQGLRNSV RMELQDLELQ LEERLLGLEE
QLRAVRMPSP FRSSALMGMC GSRSADNLSC PSPLNVMEPV TELMQEQSYL KSELGLGLGE
MGFEIPPGES SESVFSQATS ESSSVCSGPS HANRRTGVPS TASVGKPKTP LVARKKVFRA
SVALTPTAPS RTGSVQTPPD LESSEEVDAA EEAPEVVGPK SEVEEGHGKL PSMPAAEEMH
KNVEQDELQQ VIREIKESIV GEIRREIVSG LLAAVSSSKA SNSKQDNH
