ID A0A9J7MPG0_BRAFL Unreviewed; 472 AA.
AC A0A9J7MPG0;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE SubName: Full=Protein kinase C and casein kinase substrate in neurons protein 1-like isoform X6 {ECO:0000313|RefSeq:XP_035674615.1};
GN Name=LOC118414577 {ECO:0000313|RefSeq:XP_035674615.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554, ECO:0000313|RefSeq:XP_035674615.1};
RN [1] {ECO:0000313|Proteomes:UP000001554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|Proteomes:UP000001554};
RX PubMed=32313176;
RA Simakov O., Marletaz F., Yue J.X., O'Connell B., Jenkins J., Brandt A.,
RA Calef R., Tung C.H., Huang T.K., Schmutz J., Satoh N., Yu J.K.,
RA Putnam N.H., Green R.E., Rokhsar D.S.;
RT "Deeply conserved synteny resolves early events in vertebrate evolution.";
RL Nat. Ecol. Evol. 0:0-0(2020).
RN [2] {ECO:0000313|RefSeq:XP_035674615.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035674615.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035674615.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Plays a role in endocytosis and regulates internalization of
CC plasma membrane proteins. Overexpression impairs internalization of
CC SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and
CC TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel
CC activity. {ECO:0000256|ARBA:ARBA00055545}.
CC -!- SUBUNIT: Homodimer. May form heterooligomers with other PACSINs.
CC Interacts (via SH3 domain) with DNM1, SYNJ1 and WASL. Interacts with
CC TRPV4. {ECO:0000256|ARBA:ARBA00064966}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endomembrane system
CC {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004184}.
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DR RefSeq; XP_035674615.1; XM_035818722.1.
DR GeneID; 118414577; -.
DR Proteomes; UP000001554; Chromosome 4.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR CDD; cd07655; F-BAR_PACSIN; 1.
DR CDD; cd11843; SH3_PACSIN; 1.
DR FunFam; 2.30.30.40:FF:000014; Kinase C and casein kinase substrate in neurons protein; 1.
DR FunFam; 1.20.1270.60:FF:000009; Protein kinase C and casein kinase substrate in neurons 2; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF11; SYNDAPIN, ISOFORM C; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|PROSITE-
KW ProRule:PRU01077}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 13..284
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 414..472
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 334..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 54117 MW; C458AC4ECAC512C3 CRC64;
MSNYAPSDEG SLPQPSSDSF WEVGNYKTTV KRMEDGYRLC NELMTMVKER CEIEKSYAKA
LKHWAKKWNK SVEEGPEYGT MSSGWKSFCT EAERVHDLHM EVRDKLISDI QEEVASWQKE
NYKKLMMTGF KETKEADDAF RKAQKPWAKM LQRVNQSKKA YHTACRNEKT AINAENNGKK
DTSISPDKVK ALRDRVEKCK AETTKTKDKY DKTLQEINGY NAKYMEDMTL QFQKCQDFEE
KRLQFFKQTL LNMHQCLDLS VEQRFPQIYT DLQQSIVKVE SGQDLKFWAK NHGTEMGMNW
PQFEEYNPEL RAITKKSKKN VANEGITMTN ITPLTENYQP NSYHHQQAQD SQNSSGSVDD
YDDTKNPFAE DDNPTSKASS RPTSNTSNAA EWSDEDEANP FTNGGGGSGT GDAEVGVPVR
ALYDYEGQED DELTFKAGDL LTKLEDEDEQ GWCKGKFRGR VGLYPANYVE PV
//
