ID A0A2K6FCT3_PROCO Unreviewed; 515 AA.
AC A0A2K6FCT3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000011796.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000011796.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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DR AlphaFoldDB; A0A2K6FCT3; -.
DR STRING; 379532.ENSPCOP00000011796; -.
DR Ensembl; ENSPCOT00000022386.1; ENSPCOP00000011796.1; ENSPCOG00000017426.1.
DR GeneTree; ENSGT00950000182767; -.
DR OMA; HEYAKEE; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR CDD; cd11893; SH3_MIA3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23158; MELANOMA INHIBITORY ACTIVITY-RELATED; 1.
DR PANTHER; PTHR23158:SF54; TRANSPORT AND GOLGI ORGANIZATION PROTEIN 1 HOMOLOG; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..515
FT /note="SH3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014331218"
FT DOMAIN 45..107
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 154..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 57511 MW; EDC88532D6477CB1 CRC64;
MAAAPALLLW LLAAGAPWRV RGLRDPGAGR RFSEQKLCAD GECSMLMYRG EALEDFTGPD
CRFVNFKKGD PVYVYYKLAG RGPEVWAGSV GRIFGYFPKD LIQVVHEYTK EELQVPTDET
DFVCFDGGRD DFDNYNVEEL LGFLELYDSA AAESEKAIEE TEHMEKPPEV SNESEAEPVE
ANPEESESVF SENTEDLKEP FMDQKNHPQA NSQAGNAQGE QPSFEPFDEM LQDKLKVPES
ENNKTSNSSQ VSNEQKKVDA YKLLKKEMTL DLKTKFGSTA DALVSDDETT SLVTSLEDDF
DEELDAEYYA VEKKEEENPE DFDELPLLTF MSREDTETPA RSGVEKCSSD KGQNSNEKDK
VKGIVSPGIK NDDTNILTTR GDTIFSIVTG GEEKTGVMDL ESSDSEEEKE DDDASVPGST
QEKPRSTTDH TDPEDEEDGL LIVEVPKTNN DKDTEVDTGL HIKGKGRKVQ EPERGPVQDG
TELEDEKQEG PVLLLLWCLT LHNGFKFNPG KYKRC
//
