ID S2JXI2_MUCC1 Unreviewed; 1152 AA.
AC S2JXI2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=HMPREF1544_08715 {ECO:0000313|EMBL:EPB84550.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB84550.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC required for the internalization of endosomes during actin-coupled
CC endocytosis. The complex links the site of endocytosis to the cell
CC membrane-associated actin cytoskeleton. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization.
CC {ECO:0000256|ARBA:ARBA00025194}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SLA1 family.
CC {ECO:0000256|ARBA:ARBA00007948}.
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DR EMBL; KE124036; EPB84550.1; -; Genomic_DNA.
DR AlphaFoldDB; S2JXI2; -.
DR STRING; 1220926.S2JXI2; -.
DR VEuPathDB; FungiDB:HMPREF1544_08715; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR InParanoid; S2JXI2; -.
DR OMA; GENTTHE; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000014254; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd11773; SH3_Sla1p_1; 1.
DR CDD; cd22249; UDM1_RNF168_RNF169-like; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR Gene3D; 2.30.30.700; SLA1 homology domain 1; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR007131; SHD1.
DR InterPro; IPR035800; Sla1_SH3_1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR Pfam; PF03983; SHD1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 3.
PE 3: Inferred from homology;
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Reference proteome {ECO:0000313|Proteomes:UP000014254};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 2..66
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 68..128
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 310..371
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 379..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1152 AA; 126498 MW; 054A82E300DD7922 CRC64;
MKYVAICVAL YDYQAQVDDE ELSFNADDVL YILENNDPDW YKAQLKVPSA PDGGPIGIIP
SNYVEKAKPI GSVKAIYDYQ PQSIEEVEFK EDEVLALYEN DDPDWFVVEK SNGDIGLAPS
NYVEQQEQGA TNVEKPLPAV ANASPLLAAP TTSTTAAASP VLNRSDSALS WSVHEYDVIK
KKKTKSKGNL MVGNGMFCYG SETDKASPVR QFQVNQVLTA SIDGKNVHIE MNDAQHSVFD
FQTASQSEAK GILTKIESSK TASNAAVGLA LPSPAAMTTS TSPVSVHTPA PAPAPPVIEE
SASVNGASAC EPRWAIALFA FKPEADEETY LEEHEQVLIT DYISSTDWWT IEHKDGTAGI
VPANYVKFQD EYEADLRAEE AEEEKKRSEA AAAAARQAEI AAKEKQQREM EEKERKRKEE
EDQREKQRQK EMAELNRQRD LEEKERARQA EVDRRRKMQE EAKQRELDAK KQANLAATTM
ASPQMGGGSP RRSQIPAPPP PPPALSSHTA SSPSLPTYNQ QPAAPKHTDP NKPDPAKVRM
WTDRTGAFKV EAQFLSCANG KIRLFKTNGV KIDVPTQKMC IEDLKYIEQE TGIKQYEDTN
DNIPLAQLNN NSKFSWFDYF KKANLPHSAC VEYAGNFDAN KLTEQDVERL THRKMKLLGM
SEKHVQRIQR FIETNQAEPP SDNEGARPGG LARPKMKVKK SVTFGAVSYI HEDGDSDNDD
DVQWQIQQDE ILARQLQEQE QHSGGGSSSL HRRGTGRPTP SHSAPRDVNS SVLTPQQFEP
LKPVQAAPVQ SPPQQQREIT PLTALPVQNN NTAPPPPPKP AFEDDAWAPR AGSSPSVQAA
TASPAWNATQ RSNTLPANVS SPARQRPTAQ LSQQSMVDPQ LLAKWGGSPA LAAANSRPVP
PPPTSAAIAT PNNTNFAPLQ RSATMQPQTT GFQPQGSMTS LPTMLNQASN ASLPTLQPQA
SMTSLPQTQQ VPATPSFVNN GFQQQQQPTG TSFSSPSVQQ PQFTNNNSSS SLNQYMYNQP
SPHVVPLQSV LPPPLAPQLT ASSYQSTVSS FGSPQIQPQT TGRNWANATP DNPFGSGALN
NPAMMQQQQQ PNYGMPPQNT GFVPQQQYGN HTQIDPTDKY AVFKTVNTST PSVFSNQQQQ
QQPPQQQRSF YY
//
