ID A0A3B5QY55_XIPMA Unreviewed; 1205 AA.
AC A0A3B5QY55;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=SEC24 homolog C, COPII coat complex component {ECO:0000313|Ensembl:ENSXMAP00000035822.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000035822.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000035822.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000035822.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, COPII-coated
CC vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane
CC protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}. 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 SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000256|ARBA:ARBA00008334}.
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DR AlphaFoldDB; A0A3B5QY55; -.
DR Ensembl; ENSXMAT00000030663.1; ENSXMAP00000035822.1; ENSXMAG00000015879.2.
DR GeneTree; ENSGT00950000182924; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd01479; Sec24-like; 1.
DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR006900; Sec23/24_helical_dom.
DR InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR InterPro; IPR006896; Sec23/24_trunk_dom.
DR InterPro; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR13803:SF5; PROTEIN TRANSPORT PROTEIN SEC24C; 1.
DR PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF08033; Sec23_BS; 1.
DR Pfam; PF04815; Sec23_helical; 1.
DR Pfam; PF04811; Sec23_trunk; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 535..573
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 612..856
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 861..944
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 957..1056
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 1075..1145
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 57..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1205 AA; 131051 MW; 602170F72D4523D6 CRC64;
MWTWHSVAAV PLNVRFCYQE GIREQHPGTA SSSVGHRASP FATNNGLPYY LHLYRGQARG
PPTSAPPPVS APQQYNQYSH SQGDMQNGPP PMTQAPPRPA AAQSYNQGHM NMTGPHPSYP
QHYGPPPTMQ QVTSQMTGMQ ITSGPPTPAG PGYAPPHSSQ PPISTYSAPP QPSYTQAPPP
ASSAPTQPPP PGVPAASQQY YGVPPLPSQQ PFDSSRPPTS QQQFTSSAPP PPSQQTFPPS
SFSGPPTRPQ AAPVSQPQPP FSAAPPSLSS APPPGSQPGF AGGPPPIAQG SFPPQLTPPS
SQPGSFPPPG PPPTSAASGQ YPPMSQPQQP PAAQPSPYHS GPPPPRAQMP PTSMGQSNHL
PPGPQGPLGQ QGPPGPLQQP PVQPGMQTGY PPQQNGAFGQ ARSPQPGYAG PYPGQPNYGA
PAPAPTAAPA PQKRLDPDAI PSPIQVIEDD KAKSNEPFTT GVRGQAPPLV TTNFQVKDQG
NASPRFIRCT AYNMPCTSDM AKQSQVPLAA VIKPLATLPP DEAPPYVVDH GETGPIRCNR
CKAYMCPYMQ FIEGGRRFQC GFCSCVTEVP PHYFQHLDHT GKRVDCYDRP ELSLGSYEYL
ATVDYCKNNK LPQPPAFIFL IDVSYNAVKS GMVSIICNEL KSLLDLLPRQ NPEVDSVIRV
GFVTYNKVLH FYNVKSTLAQ PQMLVVSDVS DMFVPLLDGF LVNVNESRQV IESLLDQIPE
MFADTRETET VFGPVIQAGL EALKAADCAG KLFVFHTSLP IAEAPGKLKN REDKKLIGTD
KEKTLFQPQV GVYNNLAKEC VAQGCCVDLF LFPNQYVDVA TLGVVPVSTG GSIYKYTYFQ
AQTDQERFLN DLRRDVQKQV GFDAVMRVRT STGIRATDFF GSFYMNNTTD VELAGLDCDK
AITVEFKHDD KLSEETGALM QCAVLYTSCS GQRRLRIHNM AVNCCAQLAD LYRNCETDTI
INYFAKYAFR GVANNPTKAV RDTLVNQCAQ ILACYRKNCA SPSSAGQLIL PECMKLLPVY
LNCVMKSDVL LPGADVSLDD RAYLKQLIGC MDVAETHVFF YPRLLPVMKL ESGSLPVAVR
DSEERLSKGG VYLMETGLHL FLWVGASVQQ ELLLNIFGTP SFSQIDPNMI SLPVLDNPFS
QRLREVVDSF RAQRSRYMKL MVVKQEDRAE LTFRHFLVED KSASGGASYV DFLCHMHKEI
RQLLS
//
