ID   CT2NL_PONAB             Reviewed;         639 AA.
AC   Q5RDH2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=CTTNBP2 N-terminal-like protein;
GN   Name=CTTNBP2NL;
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   -!- FUNCTION: Regulates lamellipodial actin dynamics in a CTTN-dependent
CC       manner. {ECO:0000250|UniProtKB:Q8SX68}.
CC   -!- SUBUNIT: May form homomers (By similarity). May interact with MOB4,
CC       PPP2R1A, PPP2CB, STK24, STK25, STK26, STRN4, STRIP1 and STRIP2.
CC       Interacts with CTTN/cortactin; this interaction may redistribute CTTN
CC       to stress fibers (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC       {ECO:0000250|UniProtKB:Q8SX68}. Cytoplasm, cytoskeleton, stress fiber
CC       {ECO:0000250|UniProtKB:Q99LJ0}.
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DR   EMBL; CR857938; CAH90185.1; -; mRNA.
DR   RefSeq; NP_001125066.1; NM_001131594.1.
DR   AlphaFoldDB; Q5RDH2; -.
DR   SMR; Q5RDH2; -.
DR   STRING; 9601.ENSPPYP00000001193; -.
DR   Ensembl; ENSPPYT00000039457; ENSPPYP00000036870; ENSPPYG00000001024.
DR   GeneID; 100171947; -.
DR   KEGG; pon:100171947; -.
DR   CTD; 55917; -.
DR   eggNOG; KOG1103; Eukaryota.
DR   GeneTree; ENSGT00950000182852; -.
DR   HOGENOM; CLU_028813_1_0_1; -.
DR   InParanoid; Q5RDH2; -.
DR   OrthoDB; 660559at2759; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019131; Cortactin-binding_p2_N.
DR   Pfam; PF09727; CortBP2; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..639
FT                   /note="CTTNBP2 N-terminal-like protein"
FT                   /id="PRO_0000234539"
FT   REGION          387..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          511..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          87..285
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        409..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..591
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         523
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         527
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         560
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         563
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         568
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         570
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         590
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
FT   MOD_RES         592
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9P2B4"
SQ   SEQUENCE   639 AA;  70168 MW;  1EB73612173F40B3 CRC64;
     MNLEKLSKPE LLTLFSILEG ELEARDLVIE ALKAQHRDTF IEERYGKYNI SDPLMALQRD
     FETLKEKNDG EKQPVCTNPL SILKVVMKQC KNMQERMLSQ LAAAESRHRK VILDLEEERQ
     RHAQDTAEGD DVTYMLEKER ERLTQQLEFE KSQVKKFEKE QKKLSSQLEE ERSRHKQLSS
     MLVLECKKAT NKAAEEGQKA GELSLKLEKE KSRVSKLEEE LAAERKRGLQ TEAQVEKQLS
     EFDIEREQLR AKLNREENRT KTLKEEMESL KKIVKDLEAS HQHSSPNEQL KKPVTVSKGT
     ATEPLMLMSV FCQTESFPAE RTHGSNIAKM TNTGLPGPAT PAYSYAKTNG HCDPEIQTTR
     ELTAGNNVEN QVPPREKSVA LAQEKPVENG GCPVGIETPV PMPSPLPSSG SSLSPSSTAS
     SSLTSSPCSS PVLTKRLLGS SASSPGYQSS YQVGINQRFH AARHKFQSQA DQDQQASGLQ
     SPPSRDLSPT LIDNSAAKQL ARNTVTQVLS RFTSQQGPIK PVSPNSSPFG TDYRNLANTA
     NPRGDTSHSP TPGKVSSPLS PLSPGIKSPT IPRAERGNPP PIPPKKPGLT PSPSATTPLT
     KTHSQAASLT TAEDLASSCS SNTVVANGKD VELLLPTSS