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Protein

Protein transport protein Sec23A

Gene

SEC23A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi61ZincCombined sources1
Metal bindingi66ZincCombined sources1
Metal bindingi85ZincCombined sources1
Metal bindingi88ZincCombined sources1

GO - Molecular functioni

  • zinc ion binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processER-Golgi transport, Protein transport, Transport
LigandMetal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1655829 Regulation of cholesterol biosynthesis by SREBP (SREBF)
R-HSA-204005 COPII-mediated vesicle transport
R-HSA-2132295 MHC class II antigen presentation
R-HSA-5694530 Cargo concentration in the ER
R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC

Names & Taxonomyi

Protein namesi
Recommended name:
Protein transport protein Sec23ACurated
Short name:
hSec23A1 Publication
Alternative name(s):
SEC23-related protein A
Gene namesi
Name:SEC23AImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000100934.14
HGNCiHGNC:10701 SEC23A
MIMi610511 gene
neXtProtiNX_Q15436

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Craniolenticulosutural dysplasia (CLSD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects.
See also OMIM:607812
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031030382F → L in CLSD; loss of COPII vesicle coating; results in absence of incorporation of cargo proteins into vesicles. 1 PublicationCorresponds to variant dbSNP:rs118204000EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi628F → A: Decreased interaction with MIA3; when associated with A-681. 1 Publication1
Mutagenesisi672Y → K: Decreased interaction with MIA3; when associated with A-678. 1 Publication1
Mutagenesisi678Y → A: Decreased interaction with MIA3; when associated with K-672. 1 Publication1
Mutagenesisi681F → A: Decreased interaction with MIA3; when associated with A-628. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi10484
MalaCardsiSEC23A
MIMi607812 phenotype
OpenTargetsiENSG00000100934
Orphaneti50814 Craniolenticulosutural dysplasia
PharmGKBiPA35624

Polymorphism and mutation databases

BioMutaiSEC23A
DMDMi143811354

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002051462 – 765Protein transport protein Sec23AAdd BLAST764

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Modified residuei308PhosphothreonineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15436
MaxQBiQ15436
PaxDbiQ15436
PeptideAtlasiQ15436
PRIDEiQ15436
ProteomicsDBi60595

PTM databases

iPTMnetiQ15436
PhosphoSitePlusiQ15436
SwissPalmiQ15436

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000100934
CleanExiHS_SEC23A
ExpressionAtlasiQ15436 baseline and differential
GenevisibleiQ15436 HS

Organism-specific databases

HPAiHPA043806
HPA069974

Interactioni

Subunit structurei

COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and Sar1 (PubMed:17499046). Interacts with SEC23IP. Interacts with HTR4 (By similarity). Interacts with SEC16A (PubMed:17192411). Interacts with SLC6A4 (By similarity). Interacts (as part of the Sec23/24 complex) with SEC22B; recruits SEC22B into COPII-coated vesicles and allows the transport of this cargo from the endoplasmic reticulum to the Golgi (PubMed:17499046). Interacts (via Gelsolin-like repeat) with CTAGE5 and MIA3; specifically involved in the transport of large cargos like the collagen COL7A1 (PubMed:27551091).By similarity3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi115747, 87 interactors
IntActiQ15436, 57 interactors
MINTiQ15436
STRINGi9606.ENSP00000306881

Structurei

Secondary structure

1765
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 15Combined sources12
Beta strandi16 – 24Combined sources9
Helixi28 – 31Combined sources4
Beta strandi34 – 36Combined sources3
Beta strandi39 – 42Combined sources4
Beta strandi49 – 51Combined sources3
Turni64 – 66Combined sources3
Beta strandi74 – 77Combined sources4
Turni78 – 81Combined sources4
Beta strandi82 – 84Combined sources3
Beta strandi86 – 88Combined sources3
Beta strandi91 – 93Combined sources3
Helixi96 – 98Combined sources3
Beta strandi103 – 105Combined sources3
Helixi108 – 110Combined sources3
Helixi112 – 114Combined sources3
Beta strandi115 – 121Combined sources7
Beta strandi130 – 136Combined sources7
Helixi141 – 155Combined sources15
Beta strandi163 – 179Combined sources17
Turni181 – 183Combined sources3
Beta strandi185 – 190Combined sources6
Helixi198 – 204Combined sources7
Beta strandi228 – 232Combined sources5
Helixi233 – 246Combined sources14
Helixi264 – 278Combined sources15
Beta strandi285 – 292Combined sources8
Beta strandi296 – 299Combined sources4
Helixi313 – 317Combined sources5
Helixi324 – 341Combined sources18
Beta strandi344 – 350Combined sources7
Helixi357 – 360Combined sources4
Helixi362 – 366Combined sources5
Beta strandi371 – 375Combined sources5
Beta strandi377 – 379Combined sources3
Helixi380 – 388Combined sources9
Beta strandi401 – 410Combined sources10
Beta strandi414 – 422Combined sources9
Beta strandi431 – 433Combined sources3
Beta strandi439 – 442Combined sources4
Beta strandi444 – 451Combined sources8
Beta strandi457 – 463Combined sources7
Beta strandi467 – 469Combined sources3
Beta strandi477 – 487Combined sources11
Beta strandi488 – 490Combined sources3
Beta strandi492 – 501Combined sources10
Helixi506 – 508Combined sources3
Helixi509 – 515Combined sources7
Helixi519 – 534Combined sources16
Helixi542 – 557Combined sources16
Beta strandi558 – 561Combined sources4
Helixi565 – 567Combined sources3
Turni572 – 576Combined sources5
Helixi577 – 586Combined sources10
Turni588 – 590Combined sources3
Helixi592 – 594Combined sources3
Helixi597 – 607Combined sources11
Helixi612 – 619Combined sources8
Beta strandi622 – 626Combined sources5
Beta strandi628 – 631Combined sources4
Beta strandi633 – 635Combined sources3
Helixi639 – 641Combined sources3
Beta strandi647 – 651Combined sources5
Beta strandi653 – 660Combined sources8
Helixi662 – 670Combined sources9
Turni671 – 674Combined sources4
Helixi676 – 678Combined sources3
Helixi679 – 698Combined sources20
Beta strandi699 – 701Combined sources3
Beta strandi704 – 709Combined sources6
Helixi713 – 715Combined sources3
Helixi716 – 721Combined sources6
Helixi749 – 760Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NUPX-ray2.80A1-765[»]
2NUTX-ray2.30A1-765[»]
2YRCNMR-A57-108[»]
2YRDNMR-A57-108[»]
3EFOX-ray2.70A1-765[»]
3EG9X-ray3.00A1-764[»]
3EGDX-ray2.70A1-764[»]
3EGXX-ray3.30A1-764[»]
5KYNX-ray2.55A/B1-765[»]
5KYUX-ray3.51A1-765[»]
5KYWX-ray3.20A1-765[»]
5KYXX-ray3.52A1-765[»]
5KYYX-ray3.40A1-765[»]
5VNEX-ray2.70A1-764[»]
5VNFX-ray2.41A1-764[»]
5VNGX-ray2.60A1-764[»]
5VNHX-ray2.60A1-764[»]
5VNIX-ray2.79A1-764[»]
5VNJX-ray2.81A1-764[»]
5VNKX-ray2.55A1-764[»]
5VNLX-ray2.39A1-764[»]
5VNMX-ray2.77A1-764[»]
5VNNX-ray2.50A1-764[»]
5VNOX-ray2.90A1-764[»]
ProteinModelPortaliQ15436
SMRiQ15436
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15436

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati632 – 718Gelsolin-likeSequence analysisAdd BLAST87

Domaini

The Gelsolin-like repeat mediates interaction with proteins containing PPP motifs that include CTAGE5, MIA3 but also SEC31A. These interactions are probably competitive.1 Publication

Sequence similaritiesi

Belongs to the SEC23/SEC24 family. SEC23 subfamily.Curated

Phylogenomic databases

eggNOGiKOG1986 Eukaryota
COG5047 LUCA
GeneTreeiENSGT00390000006916
HOGENOMiHOG000231690
HOVERGENiHBG055039
InParanoidiQ15436
KOiK14006
OMAiQVHEIGY
OrthoDBiEOG091G063R
PhylomeDBiQ15436
TreeFamiTF300693

Family and domain databases

CDDicd11287 Sec23_C, 1 hit
Gene3Di3.40.20.10, 1 hit
3.40.50.410, 1 hit
InterProiView protein in InterPro
IPR029006 ADF-H/Gelsolin-like_dom_sf
IPR007123 Gelsolin-like_dom
IPR036180 Gelsolin-like_dom_sf
IPR037364 Sec23
IPR006900 Sec23/24_helical_dom
IPR036175 Sec23/24_helical_dom_sf
IPR006896 Sec23/24_trunk_dom
IPR012990 Sec23_24_beta_S
IPR037550 Sec23_C
IPR036465 vWFA_dom_sf
IPR006895 Znf_Sec23_Sec24
IPR036174 Znf_Sec23_Sec24_sf
PANTHERiPTHR11141 PTHR11141, 1 hit
PfamiView protein in Pfam
PF00626 Gelsolin, 1 hit
PF08033 Sec23_BS, 1 hit
PF04815 Sec23_helical, 1 hit
PF04811 Sec23_trunk, 1 hit
PF04810 zf-Sec23_Sec24, 1 hit
SUPFAMiSSF53300 SSF53300, 1 hit
SSF81811 SSF81811, 1 hit
SSF82754 SSF82754, 1 hit
SSF82919 SSF82919, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15436-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTTYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPVAA LFTPLKERPD
60 70 80 90 100
LPPIQYEPVL CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPSYAG
110 120 130 140 150
ISELNQPAEL LPQFSSIEYV VLRGPQMPLI FLYVVDTCME DEDLQALKES
160 170 180 190 200
MQMSLSLLPP TALVGLITFG RMVQVHELGC EGISKSYVFR GTKDLSAKQL
210 220 230 240 250
QEMLGLSKVP LTQATRGPQV QQPPPSNRFL QPVQKIDMNL TDLLGELQRD
260 270 280 290 300
PWPVPQGKRP LRSSGVALSI AVGLLECTFP NTGARIMMFI GGPATQGPGM
310 320 330 340 350
VVGDELKTPI RSWHDIDKDN AKYVKKGTKH FEALANRAAT TGHVIDIYAC
360 370 380 390 400
ALDQTGLLEM KCCPNLTGGY MVMGDSFNTS LFKQTFQRVF TKDMHGQFKM
410 420 430 440 450
GFGGTLEIKT SREIKISGAI GPCVSLNSKG PCVSENEIGT GGTCQWKICG
460 470 480 490 500
LSPTTTLAIY FEVVNQHNAP IPQGGRGAIQ FVTQYQHSSG QRRIRVTTIA
510 520 530 540 550
RNWADAQTQI QNIAASFDQE AAAILMARLA IYRAETEEGP DVLRWLDRQL
560 570 580 590 600
IRLCQKFGEY HKDDPSSFRF SETFSLYPQF MFHLRRSSFL QVFNNSPDES
610 620 630 640 650
SYYRHHFMRQ DLTQSLIMIQ PILYAYSFSG PPEPVLLDSS SILADRILLM
660 670 680 690 700
DTFFQILIYH GETIAQWRKS GYQDMPEYEN FRHLLQAPVD DAQEILHSRF
710 720 730 740 750
PMPRYIDTEH GGSQARFLLS KVNPSQTHNN MYAWGQESGA PILTDDVSLQ
760
VFMDHLKKLA VSSAA
Length:765
Mass (Da):86,161
Last modified:March 6, 2007 - v2
Checksum:i128DF9964B253313
GO
Isoform 2 (identifier: Q15436-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-202: Missing.

Note: No experimental confirmation available.
Show »
Length:563
Mass (Da):63,101
Checksum:iC50E45D0FC9B7300
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti623L → M in AAH36649 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031029211L → V3 PublicationsCorresponds to variant dbSNP:rs8018720Ensembl.1
Natural variantiVAR_031030382F → L in CLSD; loss of COPII vesicle coating; results in absence of incorporation of cargo proteins into vesicles. 1 PublicationCorresponds to variant dbSNP:rs118204000EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0562301 – 202Missing in isoform 2. 1 PublicationAdd BLAST202

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97064 mRNA Translation: CAA65774.1
AK127355 mRNA Translation: BAG54494.1
AK312259 mRNA Translation: BAG35191.1
AL109628 Genomic DNA No translation available.
BC036649 mRNA Translation: AAH36649.1
CCDSiCCDS9668.1 [Q15436-1]
PIRiT09574
RefSeqiNP_006355.2, NM_006364.3 [Q15436-1]
UniGeneiHs.272927

Genome annotation databases

EnsembliENST00000307712; ENSP00000306881; ENSG00000100934 [Q15436-1]
ENST00000537403; ENSP00000444193; ENSG00000100934 [Q15436-2]
GeneIDi10484
KEGGihsa:10484
UCSCiuc001wup.2 human [Q15436-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiSC23A_HUMAN
AccessioniPrimary (citable) accession number: Q15436
Secondary accession number(s): B2R5P4, B3KXI2, Q8NE16
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 6, 2007
Last modified: June 20, 2018
This is version 176 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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